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Team:Paris/Addressing overview4
From 2009.igem.org
Adressin the message in the outer membrane : OmpA
Outer membrane protein A (OmpA) is a major protein in the Escherichia coli outer membrane. OmpA plays a vital structural role in E. coli, and suggested that a perfect β-barrel structure of OmpA is important for outer membrane stability [http://www.ncbi.nlm.nih.gov/pubmed/11906175[1]]. OmpA is the most well-studied outer membrane protein in Escherichia coli. This 325-residue protein was thought to contain two domains. The classic N-terminal domain, consisting of 171 amino acid residues, was shown to cross the membrane eight times in antiparallel β-strands with four relatively large and hydrophilic surface-exposed loops and short periplasmic turns [http://www.ncbi.nlm.nih.gov/pubmed/11276254[2]]. The C-terminal domain is located in the periplasm, and binds to the peptidoglycan thus connecting it to the outer membrane [http://www.ncbi.nlm.nih.gov/pubmed/8577259[3]]. The function of OmpA is thought to contribute to the structural integrity of the outer membrane along with murein lipoprotein (4) and peptidoglycanassociated lipoprotein . In addition to its structural role, OmpA serves as a receptor of colicin and several phages (5), and it is required in F-conjugation (6,7)
Bibliography:
[http://www.ncbi.nlm.nih.gov/pubmed/11906175[1]] Ying Wang, (2002) The Function of OmpA in Escherichia coli, Biochem Biophys Res Commun.292(2):396-401
[http://www.ncbi.nlm.nih.gov/pubmed/11276254[2]] Arora, A., Abildgaard, F., Bushweller, J. H., and Tamm, L. K. (2001) Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol 8, 334–338.
[http://www.ncbi.nlm.nih.gov/pubmed/8577259[3]] Koebnik, R. (1995) Proposal for a peptidoglycan associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol. Microbiol. 16, 1269–1270.
4- Braun, V., and Bosch, V. (1972) Sequence of the mureinlipoprotein and the attachment site of the lipid. Eur. J. Biochem. 28, 51–69.
5- Lazzaroni, J.-C., and Portalier, R. (1992) The excC gene of Escherichia coli K-12 required for cell envelope integrity encodes the peptidoglycan-associated lipoprotein. Mol. Microbiol. 6, 735–742.
6- Schweizer, M., and Henning, U. (1977) Action of major outer cell envelope membrane protein in conjugation of Escherichia coli K-12. J. Bacteriol. 129, 1651–1652.
7- Koebnik, R. (1999) Structural and functional roles of the surfaceexposed loops of the β-barrel membrane protein OmpA from Escherichia coli. J. Bacteriol. 181, 3688–3694.
