1ild: Difference between revisions

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-[[Image:1ild.gif|left|200px]]
- {{Structure
+==OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6==
-|PDB= 1ild |SIZE=350|CAPTION= <scene name='initialview01'>1ild</scene>, resolution 2.8&Aring;
+<StructureSection load='1ild' size='340' side='right'caption='[[1ild]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
+<table><tr><td colspan='2'>[[1ild]] 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=1ILD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ILD 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]] 2.8&#8491;</td></tr>
-|GENE= pldA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=1ild FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ild OCA], [https://pdbe.org/1ild PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ild RCSB], [https://www.ebi.ac.uk/pdbsum/1ild PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ild ProSAT]</span></td></tr>
+</table>
-'''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6'''
+== 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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/1ild_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=1ild ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
 Outer membrane phospholipase A (OMPLA) from Escherichia coli is an integral-membrane enzyme with a unique His-Ser-Asn catalytic triad. In serine proteases and serine esterases usually an Asp occurs in the catalytic triad; its role has been the subject of much debate. Here the role of the uncharged asparagine in the active site of OMPLA is investigated by structural characterization of the Asn156Ala mutant. Asparagine 156 is not involved in maintaining the overall active-site configuration and does not contribute significantly to the thermal stability of OMPLA. The active-site histidine retains an active conformation in the mutant notwithstanding the loss of the hydrogen bond to the asparagine side chain. Instead, stabilization of the correct tautomeric form of the histidine can account for the observed decrease in activity of the Asn156Ala mutant.
-==About this Structure==
+Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad.,Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW Protein Sci. 2001 Oct;10(10):1962-9. PMID:11567087<ref>PMID:11567087</ref>
-ILD 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=1ILD OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad., Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW, Protein Sci. 2001 Oct;10(10):1962-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11567087 11567087]
+</div>
+<div class="pdbe-citations 1ild" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Phospholipase A(1)]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Dekker N]]
-[[Category: Dekker, N.]]
+[[Category: Dijkstra BW]]
-[[Category: Dijkstra, B W.]]
+[[Category: Egmond MR]]
-[[Category: Eerde, J H.Van.]]
+[[Category: Kalk KH]]
-[[Category: Egmond, M R.]]
+[[Category: Kingma RL]]
-[[Category: Kalk, K H.]]
+[[Category: Snijder HJ]]
-[[Category: Kingma, R L.]]
+[[Category: Van Eerde JH]]
-[[Category: Snijder, H J.]]
-[[Category: BOG]]
-[[Category: MPD]]
-[[Category: anti-parallel beta barrel]]
-[[Category: membrane phospholipase]]
-[[Category: membrane protein]]
-[[Category: n156a]]
-[[Category: serine hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:50 2008''