Structural evidence for dimerization-regulated activation of an integral membrane phospholipase
- PMID: 10537112
- DOI: 10.1038/44890
Structural evidence for dimerization-regulated activation of an integral membrane phospholipase
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.
Similar articles
-
Energetics of outer membrane phospholipase A (OMPLA) dimerization.J Mol Biol. 2006 Apr 21;358(1):120-31. doi: 10.1016/j.jmb.2006.01.033. Epub 2006 Jan 31. J Mol Biol. 2006. PMID: 16497324
-
Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli.J Mol Biol. 2001 Jun 1;309(2):477-89. doi: 10.1006/jmbi.2001.4675. J Mol Biol. 2001. PMID: 11371166
-
Bacterial phospholipase A: structure and function of an integral membrane phospholipase.Biochim Biophys Acta. 2000 Oct 31;1488(1-2):91-101. doi: 10.1016/s1388-1981(00)00113-x. Biochim Biophys Acta. 2000. PMID: 11080680 Review.
-
Outer-membrane phospholipase A: known structure, unknown biological function.Mol Microbiol. 2000 Feb;35(4):711-7. doi: 10.1046/j.1365-2958.2000.01775.x. Mol Microbiol. 2000. PMID: 10692149 Review.
-
Activation of a covalent outer membrane phospholipase A dimer.Eur J Biochem. 2002 Apr;269(8):2178-85. doi: 10.1046/j.1432-1033.2002.02873.x. Eur J Biochem. 2002. PMID: 11985596
Cited by
-
The outer membrane phospholipase A is essential for membrane integrity and type III secretion in Shigella flexneri.Open Biol. 2016 Sep;6(9):160073. doi: 10.1098/rsob.160073. Open Biol. 2016. PMID: 27655730 Free PMC article.
-
Assembly and Maintenance of Lipids at the Bacterial Outer Membrane.Chem Rev. 2021 May 12;121(9):5098-5123. doi: 10.1021/acs.chemrev.0c00587. Epub 2020 Sep 21. Chem Rev. 2021. PMID: 32955879 Free PMC article. Review.
-
Predicting transmembrane beta-barrels in proteomes.Nucleic Acids Res. 2004 May 11;32(8):2566-77. doi: 10.1093/nar/gkh580. Print 2004. Nucleic Acids Res. 2004. PMID: 15141026 Free PMC article.
-
Structures of membrane proteins.Q Rev Biophys. 2010 Feb;43(1):65-158. doi: 10.1017/S0033583510000041. Q Rev Biophys. 2010. PMID: 20667175 Free PMC article. Review.
-
Inactivation of the Mla system and outer-membrane phospholipase A results in disrupted outer-membrane lipid asymmetry and hypervesiculation in Bordetella pertussis.Curr Res Microb Sci. 2022 Nov 12;3:100172. doi: 10.1016/j.crmicr.2022.100172. eCollection 2022. Curr Res Microb Sci. 2022. PMID: 36518166 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
