OmpA-like transmembrane domain is an evolutionarily conserved domain of bacterial outer membrane proteins. This domain consists of an eight-stranded beta barrel.[1] OmpA is the predominant cell surface antigen in enterobacteria found in about 100,000 copies per cell.[2] The expression of OmpA is tightly regulated by a variety of mechanisms. One mechanism by which OmpA expression is regulated in Vibrio species is by an antisense non-coding RNA called VrrA.[3]
The structure consists of an eight-stranded Up-And-Down Beta-Barrel. The strands are connected by four extracellular loops and three intracellular turns.[4]
Functionedit
Numerous OmpA-like membrane-spanning domains contribute to bacterial virulence by a variety of mechanisms such as binding to host cells or immune regulators such as Factor H. Notable examples include E. coli OmpA and Yersinia pestis Ail. Several of these proteins are vaccine candidates.
E. coli OmpA was shown to make specific interactions with the human glycoprotein Ecgp on brain microvascular endothelial cells.[5]Cronobactersakazakii is a food borne pathogen causing meningitis in neonates and was shown to bind fibronectin via OmpA and this played a significant role in invasion of the blood brain barrier.[6] The Y. pestis protein Ail binds to laminin and heparin, therefore allowing bacterial attachment to host cells.[7] The Borrelia afzelii protein BAPKO_0422, is an OmpA-like transmembrane domain and binds to human Factor H.[8]
^Pautsch A, Schulz GE (Nov 1998). "Structure of the outer membrane protein A transmembrane domain". Nature Structural Biology. 5 (11): 1013–7. doi:10.1038/2983. PMID 9808047. S2CID 20529728.
^Smith SG, Mahon V, Lambert MA, Fagan RP (Aug 2007). "A molecular Swiss army knife: OmpA structure, function and expression". FEMS Microbiology Letters. 273 (1): 1–11. doi:10.1111/j.1574-6968.2007.00778.x. PMID 17559395.
^Song T, Wai SN (July 2009). "A novel sRNA that modulates virulence and environmental fitness of Vibrio cholerae". RNA Biology. 6 (3): 254–8. doi:10.4161/rna.6.3.8371. PMID 19411843.
^Fernández C, Hilty C, Wider G, Güntert P, Wüthrich K (Mar 2004). "NMR structure of the integral membrane protein OmpX". Journal of Molecular Biology. 336 (5): 1211–21. doi:10.1016/j.jmb.2003.09.014. PMID 15037080.
^Prasadarao NV, Srivastava PK, Rudrabhatla RS, Kim KS, Huang SH, Sukumaran SK (Apr 2003). "Cloning and expression of the Escherichia coli K1 outer membrane protein A receptor, a gp96 homologue". Infection and Immunity. 71 (4): 1680–8. doi:10.1128/IAI.71.4.1680-1688.2003. PMC152083. PMID 12654781.
^Nair MK, Venkitanarayanan K, Silbart LK, Kim KS (May 2009). "Outer membrane protein A (OmpA) of Cronobacter sakazakii binds fibronectin and contributes to invasion of human brain microvascular endothelial cells". Foodborne Pathogens and Disease. 6 (4): 495–501. doi:10.1089/fpd.2008.0228. PMID 19415974.
^Yamashita S, Lukacik P, Barnard TJ, Noinaj N, Felek S, Tsang TM, Krukonis ES, Hinnebusch BJ, Buchanan SK (Nov 2011). "Structural insights into Ail-mediated adhesion in Yersinia pestis". Structure. 19 (11): 1672–82. doi:10.1016/j.str.2011.08.010. PMC3217190. PMID 22078566.
^Dyer A, Brown G, Stejskal L, Laity PR, Bingham RJ (2015). "The Borrelia afzelii outer membrane protein BAPKO_0422 binds human factor-H and is predicted to form a membrane-spanning β-barrel". Bioscience Reports. 35 (4): e00240. doi:10.1042/BSR20150095. PMC4613713. PMID 26181365.
This membrane protein–related article is a stub. You can help Wikipedia by expanding it.
ompa, like, transmembrane, domain, evolutionarily, conserved, domain, bacterial, outer, membrane, proteins, this, domain, consists, eight, stranded, beta, barrel, ompa, predominant, cell, surface, antigen, enterobacteria, found, about, copies, cell, expression. OmpA like transmembrane domain is an evolutionarily conserved domain of bacterial outer membrane proteins This domain consists of an eight stranded beta barrel 1 OmpA is the predominant cell surface antigen in enterobacteria found in about 100 000 copies per cell 2 The expression of OmpA is tightly regulated by a variety of mechanisms One mechanism by which OmpA expression is regulated in Vibrio species is by an antisense non coding RNA called VrrA 3 OmpA like transmembrane domainIdentifiersSymbolOmpA membranePfamPF01389Pfam clanCL0193InterProIPR000498PROSITEPDOC00819SCOP21bxw SCOPe SUPFAMTCDB1 B 6OPM superfamily26OPM protein1qjpAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryPDB1g90 A 22 195 1bxw A 22 192 1qjp A 22 192 Contents 1 Structure 2 Function 3 See also 4 ReferencesStructure editThe structure consists of an eight stranded Up And Down Beta Barrel The strands are connected by four extracellular loops and three intracellular turns 4 Function editNumerous OmpA like membrane spanning domains contribute to bacterial virulence by a variety of mechanisms such as binding to host cells or immune regulators such as Factor H Notable examples include E coli OmpA and Yersinia pestis Ail Several of these proteins are vaccine candidates E coli OmpA was shown to make specific interactions with the human glycoprotein Ecgp on brain microvascular endothelial cells 5 Cronobacter sakazakii is a food borne pathogen causing meningitis in neonates and was shown to bind fibronectin via OmpA and this played a significant role in invasion of the blood brain barrier 6 The Y pestis protein Ail binds to laminin and heparin therefore allowing bacterial attachment to host cells 7 The Borrelia afzelii protein BAPKO 0422 is an OmpA like transmembrane domain and binds to human Factor H 8 See also editOmpA domainReferences edit Pautsch A Schulz GE Nov 1998 Structure of the outer membrane protein A transmembrane domain Nature Structural Biology 5 11 1013 7 doi 10 1038 2983 PMID 9808047 S2CID 20529728 Smith SG Mahon V Lambert MA Fagan RP Aug 2007 A molecular Swiss army knife OmpA structure function and expression FEMS Microbiology Letters 273 1 1 11 doi 10 1111 j 1574 6968 2007 00778 x PMID 17559395 Song T Wai SN July 2009 A novel sRNA that modulates virulence and environmental fitness of Vibrio cholerae RNA Biology 6 3 254 8 doi 10 4161 rna 6 3 8371 PMID 19411843 Fernandez C Hilty C Wider G Guntert P Wuthrich K Mar 2004 NMR structure of the integral membrane protein OmpX Journal of Molecular Biology 336 5 1211 21 doi 10 1016 j jmb 2003 09 014 PMID 15037080 Prasadarao NV Srivastava PK Rudrabhatla RS Kim KS Huang SH Sukumaran SK Apr 2003 Cloning and expression of the Escherichia coli K1 outer membrane protein A receptor a gp96 homologue Infection and Immunity 71 4 1680 8 doi 10 1128 IAI 71 4 1680 1688 2003 PMC 152083 PMID 12654781 Nair MK Venkitanarayanan K Silbart LK Kim KS May 2009 Outer membrane protein A OmpA of Cronobacter sakazakii binds fibronectin and contributes to invasion of human brain microvascular endothelial cells Foodborne Pathogens and Disease 6 4 495 501 doi 10 1089 fpd 2008 0228 PMID 19415974 Yamashita S Lukacik P Barnard TJ Noinaj N Felek S Tsang TM Krukonis ES Hinnebusch BJ Buchanan SK Nov 2011 Structural insights into Ail mediated adhesion in Yersinia pestis Structure 19 11 1672 82 doi 10 1016 j str 2011 08 010 PMC 3217190 PMID 22078566 Dyer A Brown G Stejskal L Laity PR Bingham RJ 2015 The Borrelia afzelii outer membrane protein BAPKO 0422 binds human factor H and is predicted to form a membrane spanning b barrel Bioscience Reports 35 4 e00240 doi 10 1042 BSR20150095 PMC 4613713 PMID 26181365 nbsp This membrane protein related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title OmpA like transmembrane domain amp oldid 1170217116, wikipedia, wiki, book, books, library,
