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This family includes homologs of the well characterized OmpA protein of Escherichia coli. Members of this family (similar to members of the OprF family) show a modular architecture which is composed of two distinctstructural domains: an N-terminal ß-barrel domain formed by 8 beta strands with short turns at the periplasmic ends and long flexible loops at the external ends that anchors the protein to the outer membrane; and a C-terminal domain that protrudes into the periplasmic space interacting with peptidoglycans. The C-terminal domain (named OmpA-like domain), is also found in a number of outer membrane lipoproteins, therefore it is not characteristic of ß-barrels. OmpA is largely expressed in the outer membrane of Escherichia coli and is required for bacterial conjugation and for maintenance of outer membrane stability. There is also evidence that OmpA exhibits a small channel activity. There is a distant homology to Neisserial opacity (Opa) adhesins and members of the Ail/Lom/OmpX family but the barrels, though they possess the same number of strands (8), show different characteristics (shear numbers, inclination with respect to the membrane).
Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
Mol Microbiol. 2004 Feb;51(4):1027-37. doi: 10.1111/j.1365-2958.2003.03903.x.
OmpA membrane domain as a tight-binding anchor for lipid bilayers
Chembiochem. 2002 May 3;3(5):463-6. doi: 10.1002/1439-7633(20020503)3:5<463::AID-CBIC463>3.0.CO;2-P.
Structure of the outer membrane protein A transmembrane domain
Nat Struct Biol. 1998 Nov;5(11):1013-7. doi: 10.1038/2983.
High-resolution structure of the OmpA membrane domain
J Mol Biol. 2000 Apr 28;298(2):273-82. doi: 10.1006/jmbi.2000.3671.
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
Nat Struct Biol. 2001 Apr;8(4):334-8. doi: 10.1038/86214.
A minimal transmembrane beta-barrel platform protein studied by nuclear magnetic resonance
Biochemistry. 2007 Feb 6;46(5):1128-40. doi: 10.1021/bi061265e.
Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A
J Am Chem Soc. 2006 May 31;128(21):6947-51. doi: 10.1021/ja0608343.
Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications
J Mol Biol. 2009 Jan 9;385(1):117-30. doi: 10.1016/j.jmb.2008.10.021. Epub 2008 Oct 15.
|Proteins in this family with 3D-structure|