1QD5: OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

Citation:
Abstract
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.
PDB ID: 1QD5Download
MMDB ID: 11311
PDB Deposition Date: 1999/7/9
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.17  Å
Source Organism:
Similar Structures:
Biological Unit for 1QD5: monomeric; determined by author
Molecular Components in 1QD5
Label Count Molecule
Protein (1 molecule)
1
Outer Membrane Phospholipase a(Gene symbol: pldA)
Molecule annotation
Chemicals (5 molecules)
1
5
* Click molecule labels to explore molecular sequence information.

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