Globin superfamily members share a common three-dimensional fold.[3] This 'globin fold' typically consists of eight alpha helices, although some proteins have additional helix extensions at their termini.[4] Since the globin fold contains only helices, it is classified as an all-alpha protein fold.
The globin fold is found in its namesake globin families as well as in phycocyanins. The globin fold was thus the first protein fold discovered (myoglobin was the first protein whose structure was solved).
Helix packaging
The eight helices of the globin fold core share significant nonlocal structure, unlike other structural motifs in which amino acids close to each other in primary sequence are also close in space. The helices pack together at an average angle of about 50 degrees, significantly steeper than other helical packings such as the helix bundle. The exact angle of helix packing depends on the sequence of the protein, because packing is mediated by the sterics and hydrophobic interactions of the amino acid side chains near the helix interfaces.
Evolution
This section is missing information about M (myoglobin-like + single, 3/3), S (sensor, 3/3), and T (truncated, 2/2) families; PMID 16061809, PMID 23541529, and PMID 26788940. Please expand the section to include this information. Further details may exist on the talk page.(November 2020)
Globins evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric globins, flavohaemoglobins and globin-coupled sensors. Bacteria have all three types of globins, while archaea lack flavohaemoglobins, and eukaryotes lack globin-coupled sensors.[5][6] Several functionally different haemoglobins can coexist in the same species.
Although the fold of the globin superfamily is highly evolutionarilyconserved, the sequences that form the fold can have as low as 16% sequence identity. While the sequence specificity of the fold is not stringent, the hydrophobic core of the protein must be maintained and hydrophobic patches on the generally hydrophilic solvent-exposed surface must be avoided in order for the structure to remain stable and soluble. The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to sickle-cell anemia.
Neuroglobin: a myoglobin-like haemprotein expressed in vertebrate brain and retina, where it is involved in neuroprotection from damage due to hypoxia or ischemia.[7] Neuroglobin belongs to a branch of the globin family that diverged early in evolution.
Non-symbiotic haemoglobin (NsHb): occurs in non-leguminous plants, and can be over-expressed in stressed plants .
Flavohaemoglobins (FHb): chimeric, with an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD/FAD-binding domain. FHb provides protection against nitric oxide via its C-terminal domain, which transfers electrons to haem in the globin.[10]
Globin E: a globin responsible for storing and delivering oxygen to the retina in birds[11]
Globin-coupled sensors: chimeric, with an N-terminal myoglobin-like domain and a C-terminal domain that resembles the cytoplasmicsignalling domain of bacterial chemoreceptors. They bind oxygen, and act to initiate an aerotactic response or regulategene expression.[12][13]
Protoglobin: a single domain globin found in archaea that is related to the N-terminal domain of globin-coupled sensors.[14]
Truncated 2/2 globin: lack the first helix, giving them a 2-over-2 instead of the canonical 3-over-3 alpha-helical sandwich fold. Can be divided into three main groups (I, II and II) based on structural features.
HbN (or GlbN): a truncated haemoglobin-like protein that binds oxygen cooperatively with a very high affinity and a slow dissociation rate, which may exclude it from oxygen transport. It appears to be involved in bacterial nitric oxide detoxification and in nitrosative stress.[15]
Cyanoglobin (or GlbN): a truncated haemoprotein found in cyanobacteria that has high oxygen affinity, and which appears to serve as part of a terminal oxidase, rather than as a respiratory pigment.[16]
HbO (or GlbO): a truncated haemoglobin-like protein with a lower oxygen affinity than HbN. HbO associates with the bacterial cell membrane, where it significantly increases oxygen uptake over membranes lacking this protein. HbO appears to interact with a terminal oxidase, and could participate in an oxygen/electron-transfer process that facilitates oxygen transfer during aerobic metabolism.[17]
Glb3: a nuclear-encoded truncated haemoglobin from plants that appears more closely related to HbO than HbN. Glb3 from Arabidopsis thaliana (Mouse-ear cress) exhibits an unusual concentration-independent binding of oxygen and carbon dioxide.[18]
^Kavanaugh JS, Rogers PH, Case DA, Arnone A (April 1992). "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp----Arg: a mutation that creates an intersubunit chloride-binding site". Biochemistry. 31 (16): 4111–21. doi:10.1021/bi00131a030. PMID 1567857.
^Vinogradov SN, Hoogewijs D, Bailly X, Mizuguchi K, Dewilde S, Moens L, Vanfleteren JR (August 2007). "A model of globin evolution". Gene. 398 (1–2): 132–42. doi:10.1016/j.gene.2007.02.041. PMID 17540514.
^Branden, Carl; Tooze, John (1999). Introduction to protein structure (2nd ed.). New York: Garland Pub. ISBN978-0815323051.
^Bolognesi, M; Onesti, S; Gatti, G; Coda, A; Ascenzi, P; Brunori, M (1989). "Aplysia limacina myoglobin. Crystallographic analysis at 1.6 a resolution". Journal of Molecular Biology. 205 (3): 529–44. doi:10.1016/0022-2836(89)90224-6. PMID 2926816.
^Solène Song, Viktor Starunov, Xavier Bailly, Christine Ruta, Pierre Kerner, Annemiek J. M. Cornelissen, Guillaume Balavoine: Globins in the marine annelid Platynereis dumerilii shed new light on hemoglobin evolution in bilaterians. In: BMC Evolutionary Biology Vol. 20, Issue 165. 29 December 2020. doi:10.1186/s12862-020-01714-4. See also:
A single gene 'invented' haemoglobin several times. On: EurekAlert! 29 December 2020. Source: CNRS
^Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M (September 2003). "Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity". Structure. 11 (9): 1087–95. doi:10.1016/S0969-2126(03)00166-7. PMID 12962627.
^Fago A, Hundahl C, Malte H, Weber RE (2004). "Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins". IUBMB Life. 56 (11–12): 689–96. doi:10.1080/15216540500037299. PMID 15804833. S2CID 21182182.
^Royer WE, Omartian MN, Knapp JE (January 2007). "Low resolution crystal structure of Arenicola erythrocruorin: influence of coiled coils on the architecture of a megadalton respiratory protein". J. Mol. Biol. 365 (1): 226–36. doi:10.1016/j.jmb.2006.10.016. PMC1847385. PMID 17084861.
^Mukai M, Mills CE, Poole RK, Yeh SR (March 2001). "Flavohemoglobin, a globin with a peroxidase-like catalytic site". J. Biol. Chem. 276 (10): 7272–7. doi:10.1074/jbc.M009280200. PMID 11092893.
^Blank M, Kiger L, Thielebein A, Gerlach F, Hankeln T, Marden MC, Burmeister T (2011). "Oxygen supply from the bird's eye perspective: Globin E is a respiratory protein in the chicken retina". J. Biol. Chem. 286 (30): 26507–15. doi:10.1074/jbc.M111.224634. PMC3143615. PMID 21622558.
^Hou S, Freitas T, Larsen RW, Piatibratov M, Sivozhelezov V, Yamamoto A, Meleshkevitch EA, Zimmer M, Ordal GW, Alam M (July 2001). "Globin-coupled sensors: a class of heme-containing sensors in Archaea and Bacteria". Proc. Natl. Acad. Sci. U.S.A. 98 (16): 9353–8. Bibcode:2001PNAS...98.9353H. doi:10.1073/pnas.161185598. PMC55424. PMID 11481493.
^Freitas TA, Saito JA, Hou S, Alam M (January 2005). "Globin-coupled sensors, protoglobins, and the last universal common ancestor". J. Inorg. Biochem. 99 (1): 23–33. doi:10.1016/j.jinorgbio.2004.10.024. PMID 15598488.
^Freitas TA, Hou S, Dioum EM, Saito JA, Newhouse J, Gonzalez G, Gilles-Gonzalez MA, Alam M (April 2004). "Ancestral hemoglobins in Archaea". Proc. Natl. Acad. Sci. U.S.A. 101 (17): 6675–80. Bibcode:2004PNAS..101.6675F. doi:10.1073/pnas.0308657101. PMC404104. PMID 15096613.
^Lama A, Pawaria S, Dikshit KL (July 2006). "Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis". FEBS Lett. 580 (17): 4031–41. doi:10.1016/j.febslet.2006.06.037. PMID 16814781.
^Yeh DC, Thorsteinsson MV, Bevan DR, Potts M, La Mar GN (February 2000). "Solution 1H NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune". Biochemistry. 39 (6): 1389–99. doi:10.1021/bi992081l. PMID 10684619.
^Pathania R, Navani NK, Rajamohan G, Dikshit KL (May 2002). "Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli". J. Biol. Chem. 277 (18): 15293–302. doi:10.1074/jbc.M111478200. PMID 11796724.
^Watts RA, Hunt PW, Hvitved AN, Hargrove MS, Peacock WJ, Dennis ES (August 2001). "A hemoglobin from plants homologous to truncated hemoglobins of microorganisms". Proc. Natl. Acad. Sci. U.S.A. 98 (18): 10119–24. Bibcode:2001PNAS...9810119W. doi:10.1073/pnas.191349198. PMC56925. PMID 11526234.
This article incorporates text from the public domain Pfam and InterPro: IPR001486
January 11, 2023
globin, confused, with, globulin, globular, protein, globins, superfamily, heme, containing, globular, proteins, involved, binding, transporting, oxygen, these, proteins, incorporate, globin, fold, series, eight, alpha, helical, segments, prominent, members, i. Not to be confused with globulin or globular protein The globins are a superfamily of heme containing globular proteins involved in binding and or transporting oxygen These proteins all incorporate the globin fold a series of eight alpha helical segments Two prominent members include myoglobin and hemoglobin Both of these proteins reversibly bind oxygen via a heme prosthetic group They are widely distributed in many organisms 2 Globin family family M the Structure of deoxyhemoglobin Rothschild 37 beta Trp Arg a mutation that creates an intersubunit chloride binding site 1 IdentifiersSymbolGlobinPfamPF00042Pfam clanCL0090InterProIPR000971PROSITEPS01033SCOP21hba SCOPe SUPFAMCDDcd01040Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryBacterial like Globin family T crystal structure of truncated hemoglobin n hbn from mycobacterium tuberculosis soaked with xe atomsIdentifiersSymbolBac globinPfamPF01152Pfam clanCL0090InterProIPR001486PROSITEPDOC00933SCOP21dlw SCOPe SUPFAMCDDcd14756Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryProtoglobin family S IdentifiersSymbolProtoglobinPfamPF11563Pfam clanCL0090InterProIPR012102CDDcd01068Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Contents 1 Structure 1 1 Helix packaging 2 Evolution 2 1 Sequence conservation 3 Subfamilies 4 Examples 5 The globin fold 6 See also 7 ReferencesStructure EditGlobin superfamily members share a common three dimensional fold 3 This globin fold typically consists of eight alpha helices although some proteins have additional helix extensions at their termini 4 Since the globin fold contains only helices it is classified as an all alpha protein fold The globin fold is found in its namesake globin families as well as in phycocyanins The globin fold was thus the first protein fold discovered myoglobin was the first protein whose structure was solved Helix packaging Edit The eight helices of the globin fold core share significant nonlocal structure unlike other structural motifs in which amino acids close to each other in primary sequence are also close in space The helices pack together at an average angle of about 50 degrees significantly steeper than other helical packings such as the helix bundle The exact angle of helix packing depends on the sequence of the protein because packing is mediated by the sterics and hydrophobic interactions of the amino acid side chains near the helix interfaces Evolution EditThis section is missing information about M myoglobin like single 3 3 S sensor 3 3 and T truncated 2 2 families PMID 16061809 PMID 23541529 and PMID 26788940 Please expand the section to include this information Further details may exist on the talk page November 2020 Globins evolved from a common ancestor and can be divided into three groups single domain globins and two types of chimeric globins flavohaemoglobins and globin coupled sensors Bacteria have all three types of globins while archaea lack flavohaemoglobins and eukaryotes lack globin coupled sensors 5 6 Several functionally different haemoglobins can coexist in the same species Eight globins are known to occur in vertebrates androglobin cytoglobin globin E globin X globin Y hemoglobin myoglobin and neuroglobin Sequence conservation Edit Although the fold of the globin superfamily is highly evolutionarily conserved the sequences that form the fold can have as low as 16 sequence identity While the sequence specificity of the fold is not stringent the hydrophobic core of the protein must be maintained and hydrophobic patches on the generally hydrophilic solvent exposed surface must be avoided in order for the structure to remain stable and soluble The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule This mutation creates a hydrophobic patch on the protein surface that promotes intermolecular aggregation the molecular event that gives rise to sickle cell anemia Subfamilies EditLeghaemoglobin InterPro IPR001032 Myoglobin InterPro IPR002335 Erythrocruorin InterPro IPR002336 Hemoglobin beta InterPro IPR002337 Hemoglobin alpha InterPro IPR002338 Myoglobin trematode type InterPro IPR011406 Globin nematode InterPro IPR012085 Globin lamprey hagfish type InterPro IPR013314 Globin annelid type InterPro IPR013316 Haemoglobin extracellular InterPro IPR014610Examples EditHuman genes encoding globin proteins include CYGB HBA1 HBA2 HBB HBD HBE1 HBG1 HBG2 HBM HBQ1 HBZ MBThe globins include Haemoglobin Hb Myoglobin Mb Neuroglobin a myoglobin like haemprotein expressed in vertebrate brain and retina where it is involved in neuroprotection from damage due to hypoxia or ischemia 7 Neuroglobin belongs to a branch of the globin family that diverged early in evolution Cytoglobin an oxygen sensor expressed in multiple tissues Related to neuroglobin 8 Erythrocruorin highly cooperative extracellular respiratory proteins found in annelids and arthropods that are assembled from as many as 180 subunit into hexagonal bilayers 9 Leghaemoglobin legHb or symbiotic Hb occurs in the root nodules of leguminous plants where it facilitates the diffusion of oxygen to symbiotic bacteriods in order to promote nitrogen fixation Non symbiotic haemoglobin NsHb occurs in non leguminous plants and can be over expressed in stressed plants Flavohaemoglobins FHb chimeric with an N terminal globin domain and a C terminal ferredoxin reductase like NAD FAD binding domain FHb provides protection against nitric oxide via its C terminal domain which transfers electrons to haem in the globin 10 Globin E a globin responsible for storing and delivering oxygen to the retina in birds 11 Globin coupled sensors chimeric with an N terminal myoglobin like domain and a C terminal domain that resembles the cytoplasmic signalling domain of bacterial chemoreceptors They bind oxygen and act to initiate an aerotactic response or regulate gene expression 12 13 Protoglobin a single domain globin found in archaea that is related to the N terminal domain of globin coupled sensors 14 Truncated 2 2 globin lack the first helix giving them a 2 over 2 instead of the canonical 3 over 3 alpha helical sandwich fold Can be divided into three main groups I II and II based on structural features HbN or GlbN a truncated haemoglobin like protein that binds oxygen cooperatively with a very high affinity and a slow dissociation rate which may exclude it from oxygen transport It appears to be involved in bacterial nitric oxide detoxification and in nitrosative stress 15 Cyanoglobin or GlbN a truncated haemoprotein found in cyanobacteria that has high oxygen affinity and which appears to serve as part of a terminal oxidase rather than as a respiratory pigment 16 HbO or GlbO a truncated haemoglobin like protein with a lower oxygen affinity than HbN HbO associates with the bacterial cell membrane where it significantly increases oxygen uptake over membranes lacking this protein HbO appears to interact with a terminal oxidase and could participate in an oxygen electron transfer process that facilitates oxygen transfer during aerobic metabolism 17 Glb3 a nuclear encoded truncated haemoglobin from plants that appears more closely related to HbO than HbN Glb3 from Arabidopsis thaliana Mouse ear cress exhibits an unusual concentration independent binding of oxygen and carbon dioxide 18 The globin fold EditThe globin fold cd01067 also includes some non haem proteins Some of them are the phycobiliproteins the N terminal domain of two component regulatory system histidine kinase RsbR and RsbN See also Edit Biology portalC rich stability element Globular protein Hemoglobin Heme Myoglobin PhytoglobinReferences Edit Kavanaugh JS Rogers PH Case DA Arnone A April 1992 High resolution X ray study of deoxyhemoglobin Rothschild 37 beta Trp Arg a mutation that creates an intersubunit chloride binding site Biochemistry 31 16 4111 21 doi 10 1021 bi00131a030 PMID 1567857 Vinogradov SN Hoogewijs D Bailly X Mizuguchi K Dewilde S Moens L Vanfleteren JR August 2007 A model of globin evolution Gene 398 1 2 132 42 doi 10 1016 j gene 2007 02 041 PMID 17540514 Branden Carl Tooze John 1999 Introduction to protein structure 2nd ed New York Garland Pub ISBN 978 0815323051 Bolognesi M Onesti S Gatti G Coda A Ascenzi P Brunori M 1989 Aplysia limacina myoglobin Crystallographic analysis at 1 6 a resolution Journal of Molecular Biology 205 3 529 44 doi 10 1016 0022 2836 89 90224 6 PMID 2926816 Vinogradov SN Hoogewijs D Bailly X Arredondo Peter R Gough J Dewilde S Moens L Vanfleteren JR 2006 A phylogenomic profile of globins BMC Evol Biol 6 31 doi 10 1186 1471 2148 6 31 PMC 1457004 PMID 16600051 Solene Song Viktor Starunov Xavier Bailly Christine Ruta Pierre Kerner Annemiek J M Cornelissen Guillaume Balavoine Globins in the marine annelid Platynereis dumerilii shed new light on hemoglobin evolution in bilaterians In BMC Evolutionary Biology Vol 20 Issue 165 29 December 2020 doi 10 1186 s12862 020 01714 4 See also A single gene invented haemoglobin several times On EurekAlert 29 December 2020 Source CNRS Pesce A Dewilde S Nardini M Moens L Ascenzi P Hankeln T Burmester T Bolognesi M September 2003 Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity Structure 11 9 1087 95 doi 10 1016 S0969 2126 03 00166 7 PMID 12962627 Fago A Hundahl C Malte H Weber RE 2004 Functional properties of neuroglobin and cytoglobin Insights into the ancestral physiological roles of globins IUBMB Life 56 11 12 689 96 doi 10 1080 15216540500037299 PMID 15804833 S2CID 21182182 Royer WE Omartian MN Knapp JE January 2007 Low resolution crystal structure of Arenicola erythrocruorin influence of coiled coils on the architecture of a megadalton respiratory protein J Mol Biol 365 1 226 36 doi 10 1016 j jmb 2006 10 016 PMC 1847385 PMID 17084861 Mukai M Mills CE Poole RK Yeh SR March 2001 Flavohemoglobin a globin with a peroxidase like catalytic site J Biol Chem 276 10 7272 7 doi 10 1074 jbc M009280200 PMID 11092893 Blank M Kiger L Thielebein A Gerlach F Hankeln T Marden MC Burmeister T 2011 Oxygen supply from the bird s eye perspective Globin E is a respiratory protein in the chicken retina J Biol Chem 286 30 26507 15 doi 10 1074 jbc M111 224634 PMC 3143615 PMID 21622558 Hou S Freitas T Larsen RW Piatibratov M Sivozhelezov V Yamamoto A Meleshkevitch EA Zimmer M Ordal GW Alam M July 2001 Globin coupled sensors a class of heme containing sensors in Archaea and Bacteria Proc Natl Acad Sci U S A 98 16 9353 8 Bibcode 2001PNAS 98 9353H doi 10 1073 pnas 161185598 PMC 55424 PMID 11481493 Freitas TA Saito JA Hou S Alam M January 2005 Globin coupled sensors protoglobins and the last universal common ancestor J Inorg Biochem 99 1 23 33 doi 10 1016 j jinorgbio 2004 10 024 PMID 15598488 Freitas TA Hou S Dioum EM Saito JA Newhouse J Gonzalez G Gilles Gonzalez MA Alam M April 2004 Ancestral hemoglobins in Archaea Proc Natl Acad Sci U S A 101 17 6675 80 Bibcode 2004PNAS 101 6675F doi 10 1073 pnas 0308657101 PMC 404104 PMID 15096613 Lama A Pawaria S Dikshit KL July 2006 Oxygen binding and NO scavenging properties of truncated hemoglobin HbN of Mycobacterium smegmatis FEBS Lett 580 17 4031 41 doi 10 1016 j febslet 2006 06 037 PMID 16814781 Yeh DC Thorsteinsson MV Bevan DR Potts M La Mar GN February 2000 Solution 1H NMR study of the heme cavity and folding topology of the abbreviated chain 118 residue globin from the cyanobacterium Nostoc commune Biochemistry 39 6 1389 99 doi 10 1021 bi992081l PMID 10684619 Pathania R Navani NK Rajamohan G Dikshit KL May 2002 Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli J Biol Chem 277 18 15293 302 doi 10 1074 jbc M111478200 PMID 11796724 Watts RA Hunt PW Hvitved AN Hargrove MS Peacock WJ Dennis ES August 2001 A hemoglobin from plants homologous to truncated hemoglobins of microorganisms Proc Natl Acad Sci U S A 98 18 10119 24 Bibcode 2001PNAS 9810119W doi 10 1073 pnas 191349198 PMC 56925 PMID 11526234 This article incorporates text from the public domain Pfam and InterPro IPR001486 Retrieved from https en wikipedia org w index php title Globin amp oldid 1108909529, wikipedia, wiki, book, books, library,
