1qd6: Difference between revisions

Revision as of 06:09, 3 May 2008

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

OverviewOverview

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 StructureAbout this Structure

1QD6 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sat May 3 06:09:01 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 [[Image:1qd6.jpg|left|200px]]
- {{Structure
+<!--
-|PDB= 1qd6 |SIZE=350|CAPTION= <scene name='initialview01'>1qd6</scene>, resolution 2.10&Aring;
+The line below this paragraph, containing "STRUCTURE_1qd6", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HDS:1-HEXADECANOSULFONIC+ACID'>HDS</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(1) Phospholipase A(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.32 3.1.1.32] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1qd6|  PDB=1qd6  |  SCENE=  }}
-|RELATEDENTRY=[[1qd5|1QD5]]
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd6 OCA], [http://www.ebi.ac.uk/pdbsum/1qd6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qd6 RCSB]</span>
-}}
 '''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI'''
@@ Line 24: / Line 21: @@
 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:[http://www.ncbi.nlm.nih.gov/pubmed/10537112 10537112]
 [[Category: Escherichia coli]]
-[[Category: Phospholipase A(1)]]
 [[Category: Protein complex]]
 [[Category: Blaauw, M.]]
@@ Line 34: / Line 30: @@
 [[Category: Ubarretxena-Belandia, I.]]
 [[Category: Verheij, H M.]]
-[[Category: anti-parallel beta barrel dimer]]
+[[Category: Anti-parallel beta barrel dimer]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:09:01 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:06 2008''