1bwp: Difference between revisions

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 <StructureSection load='1bwp' size='340' side='right'caption='[[1bwp]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bwp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BWP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bwp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWP FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1-alkyl-2-acetylglycerophosphocholine_esterase 1-alkyl-2-acetylglycerophosphocholine esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.47 3.1.1.47] </span></td></tr>
+</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1bwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwp OCA], [http://pdbe.org/1bwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bwp RCSB], [http://www.ebi.ac.uk/pdbsum/1bwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwp ProSAT]</span></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=1bwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwp OCA], [https://pdbe.org/1bwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwp RCSB], [https://www.ebi.ac.uk/pdbsum/1bwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PA1B3_BOVIN PA1B3_BOVIN]] Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain.
+[https://www.uniprot.org/uniprot/PA1B3_BOVIN PA1B3_BOVIN] Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1bwp ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Platelet-activating factor acetylhydrolases (PAF-AHs) are unique PLA2s which hydrolyze the sn-2 ester linkage in PAF-like phospholipids with a marked preference for very short acyl chains, typically acetyl. The recent solution of the crystal structure of the alpha(1) catalytic subunit of isoform Ib of bovine brain intracellular PAF-AH at 1.7 A resolution paved the way for a detailed examination of the molecular basis of substrate specificity in this enzyme. The crystal structure suggests that the side chains of Thr103, Leu48 and Leu194 are involved in substrate recognition. Three single site mutants (L48A, T103S and L194A) were overexpressed and their structures were solved to 2.3 A resolution or better by X-ray diffraction methods. Enzyme kinetics showed that, compared with wild-type protein, all three mutants have higher relative activity against phospholipids with sn-2 acyl chains longer than an acetyl. However, for each of the mutants we observed an unexpected and substantial reduction in the V(max) of the reaction. These results are consistent with the model in which residues Leu48, Thr103 and Leu194 indeed contribute to substrate specificity and in addition suggest that the integrity of the specificity pocket is critical for the expression of full catalytic function, thus conferring very high substrate selectivity on the enzyme.
-Probing the substrate specificity of the intracellular brain platelet-activating factor acetylhydrolase.,Ho YS, Sheffield PJ, Masuyama J, Arai H, Li J, Aoki J, Inoue K, Derewenda U, Derewenda ZS Protein Eng. 1999 Aug;12(8):693-700. PMID:10469831<ref>PMID:10469831</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1bwp" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]]
+[[Category: Bos taurus]]
-[[Category: Bovin]]
 [[Category: Large Structures]]
-[[Category: Aoki, J]]
+[[Category: Aoki J]]
-[[Category: Arai, H]]
+[[Category: Arai H]]
-[[Category: Derewenda, U]]
+[[Category: Derewenda U]]
-[[Category: Derewenda, Z]]
+[[Category: Derewenda Z]]
-[[Category: Ho, Y S]]
+[[Category: Ho YS]]
-[[Category: Inoue, K]]
+[[Category: Inoue K]]
-[[Category: Li, J]]
+[[Category: Li J]]
-[[Category: Masuyama, J]]
+[[Category: Masuyama J]]
-[[Category: Sheffield, P J]]
+[[Category: Sheffield PJ]]
-[[Category: Acetylhydrolase hydrolase]]
-[[Category: Hydrolase]]
-[[Category: Lipid degradation]]
-[[Category: Platelet factor]]