1qd5: Difference between revisions

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OCA

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-[[Image:1qd5.jpg|left|200px]]<br /><applet load="1qd5" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1qd5, resolution 2.17&Aring;" />
-'''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI'''<br />
-==Overview==
+==OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI==
-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.
+<StructureSection load='1qd5' size='340' side='right'caption='[[1qd5]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1qd5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QD5 FirstGlance]. <br>
-QD5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with BOG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QD5 OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd5 OCA], [https://pdbe.org/1qd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qd5 RCSB], [https://www.ebi.ac.uk/pdbsum/1qd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qd5 ProSAT]</span></td></tr>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10537112 10537112]
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PA1_ECOLI 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/1qd5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qd5 ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Phospholipase A(1)]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Blaauw M]]
-[[Category: Blaauw, M.]]
+[[Category: Dekker N]]
-[[Category: Dekker, N.]]
+[[Category: Dijkstra BW]]
-[[Category: Dijkstra, B.W.]]
+[[Category: Egmond MR]]
-[[Category: Egmond, M.R.]]
+[[Category: Kalk KH]]
-[[Category: Kalk, K.H.]]
+[[Category: Snijder HJ]]
-[[Category: Snijder, H.J.]]
+[[Category: Ubarretxena-Belandia I]]
-[[Category: Ubarretxena-Belandia, I.]]
+[[Category: Verheij HM]]
-[[Category: Verheij, H.M.]]
-[[Category: BOG]]
-[[Category: anti-parallel beta barrel]]
-[[Category: membrane phospholipase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:35:24 2007''