1qd6: Difference between revisions
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==OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI== | ==OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI== | ||
<StructureSection load='1qd6' size='340' side='right' caption='[[1qd6]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1qd6' size='340' side='right'caption='[[1qd6]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qd6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QD6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1qd6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QD6 FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Large Structures]] | |||
[[Category: Blaauw, M]] | [[Category: Blaauw, M]] | ||
[[Category: Dekker, N]] | [[Category: Dekker, N]] | ||
Revision as of 13:14, 27 November 2019
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLIOUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI
Structural highlights
Function[PA1_ECOLI] Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDimerization 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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