1qd6 | pdb_00001qd6
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI
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Overview
Dimerization is a biological regulatory mechanism employed by both soluble, and membrane proteins. However, there are few structural data on the, factors that govern dimerization of membrane proteins. Outer membrane, phospholipase A (OMPLA) is an integral membrane enzyme which participates, in secretion of colicins in Escherichia coli. In Campilobacter and, Helicobacter pylori strains, OMPLA is implied in virulence. Its activity, is regulated by reversible dimerization. Here we report X-ray structures, of monomeric and dimeric OMPLA from E. coli. Dimer interactions occur, almost exclusively in the apolar membrane-embedded parts, with two, hydrogen bonds within the hydrophobic membrane area being key, interactions. Dimerization results in functional oxyanion holes and, substrate-binding pockets, which are absent in monomeric OMPLA. These, results provide a detailed view of activation by dimerization of a, membrane protein.
About this Structure
1QD6 is a Protein complex structure of sequences from Escherichia coli with CA and HDS as ligands. Active as Phospholipase A(1), with EC number 3.1.1.32 Full crystallographic information is available from OCA.
Reference
Structural evidence for dimerization-regulated activation of an integral membrane phospholipase., Snijder HJ, Ubarretxena-Belandia I, Blaauw M, Kalk KH, Verheij HM, Egmond MR, Dekker N, Dijkstra BW, Nature. 1999 Oct 14;401(6754):717-21. PMID:10537112
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