1qd5: Difference between revisions

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[[Image:1qd5.jpg|left|200px]]


{{Structure
==OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI==
|PDB= 1qd5 |SIZE=350|CAPTION= <scene name='initialview01'>1qd5</scene>, resolution 2.17&Aring;
<StructureSection load='1qd5' size='340' side='right'caption='[[1qd5]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>
<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>
|ACTIVITY= [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]  
</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>
|GENE=
<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>
}}
<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>
 
</table>
'''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI'''
== 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 ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/1qd5_consurf.spt"</scriptWhenChecked>
1QD5 is a [[Single protein]] structure of sequence from [http://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].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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]
</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: 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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:07 2008''
Retrieved from "https://proteopedia.org/1qd5"