1qd6

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(New page: 200px<br /><applet load="1qd6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qd6, resolution 2.10&Aring;" /> '''OUTER MEMBRANE PHOSP...)
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[[Image:1qd6.jpg|left|200px]]<br /><applet load="1qd6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qd6, resolution 2.10&Aring;" />
 
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'''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI==
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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.
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<StructureSection load='1qd6' size='340' side='right'caption='[[1qd6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qd6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1QD6 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HDS:1-HEXADECANOSULFONIC+ACID'>HDS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd6 OCA], [https://pdbe.org/1qd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qd6 RCSB], [https://www.ebi.ac.uk/pdbsum/1qd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qd6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/1qd6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1qd6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:10537112</ref>
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1QD6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CA and HDS as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1QD6 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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<div class="pdbe-citations 1qd6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phospholipase A(1)]]
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[[Category: Escherichia coli K-12]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Blaauw, M.]]
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[[Category: Blaauw M]]
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[[Category: Dekker, N]]
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[[Category: Dekker N]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra BW]]
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[[Category: Egmond, M.R.]]
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[[Category: Egmond MR]]
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[[Category: Kalk, K.H.]]
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[[Category: Kalk KH]]
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[[Category: Snijder, H.J.]]
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[[Category: Snijder HJ]]
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[[Category: Ubarretxena-Belandia, I.]]
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[[Category: Ubarretxena-Belandia I]]
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[[Category: Verheij, H.M.]]
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[[Category: Verheij HM]]
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[[Category: CA]]
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[[Category: HDS]]
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[[Category: anti-parallel beta barrel dimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:35:28 2007''
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Current revision

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

PDB ID 1qd6

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