1bwp

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[[Image:1bwp.gif|left|200px]]
 
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==PROBING THE SUBSTRATE SPECIFICITY OF THE INTRACELLULAR BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE==
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The line below this paragraph, containing "STRUCTURE_1bwp", creates the "Structure Box" on the page.
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<StructureSection load='1bwp' size='340' side='right'caption='[[1bwp]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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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='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>
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{{STRUCTURE_1bwp| PDB=1bwp | SCENE= }}
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</table>
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== Function ==
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[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.
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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/bw/1bwp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1bwp ConSurf].
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<div style="clear:both"></div>
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'''PROBING THE SUBSTRATE SPECIFICITY OF THE INTRACELLULAR BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE'''
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1BWP is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10469831 10469831]
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[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aoki, J.]]
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[[Category: Aoki J]]
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[[Category: Arai, H.]]
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[[Category: Arai H]]
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[[Category: Derewenda, U.]]
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[[Category: Derewenda U]]
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[[Category: Derewenda, Z.]]
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[[Category: Derewenda Z]]
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[[Category: Ho, Y S.]]
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[[Category: Ho YS]]
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[[Category: Inoue, K.]]
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[[Category: Inoue K]]
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[[Category: Li, J.]]
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[[Category: Li J]]
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[[Category: Masuyama, J.]]
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[[Category: Masuyama J]]
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[[Category: Sheffield, P J.]]
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[[Category: Sheffield PJ]]
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[[Category: Acetylhydrolase hydrolase]]
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[[Category: Lipid degradation]]
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[[Category: Platelet factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:02:47 2008''
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Current revision

PROBING THE SUBSTRATE SPECIFICITY OF THE INTRACELLULAR BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE

PDB ID 1bwp

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