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1ceh

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(New page: 200px<br /><applet load="1ceh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ceh, resolution 1.9&Aring;" /> '''STRUCTURE AND FUNCTIO...)
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[[Image:1ceh.gif|left|200px]]<br /><applet load="1ceh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ceh, resolution 1.9&Aring;" />
 
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'''STRUCTURE AND FUNCTION OF THE CATALYTIC SITE MUTANT ASP99ASN OF PHOSPHOLIPASE A2: ABSENCE OF CONSERVED STRUCTURAL WATER'''<br />
 
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==Overview==
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==STRUCTURE AND FUNCTION OF THE CATALYTIC SITE MUTANT ASP99ASN OF PHOSPHOLIPASE A2: ABSENCE OF CONSERVED STRUCTURAL WATER==
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To probe the role of the Asp-99 ... His-48 pair in phospholipase A2 (PLA2), catalysis, the X-ray structure and kinetic characterization of the mutant, Asp-99--&gt;Asn-99 (D99N) of bovine pancreatic PLA2 was undertaken. Crystals, of D99N belong to the trigonal space group P3(1)21 and were isomorphous to, the wild type (WT) (Noel JP et al., 1991, Biochemistry 30:11801-11811)., The 1.9-A X-ray structure of the mutant showed that the carbonyl group of, Asn-99 side chain is hydrogen bonded to His-48 in the same way as that of, Asp-99 in the WT, thus retaining the tautomeric form of His-48 and the, function of the enzyme. The NH2 group of Asn-99 points away from His-48., In contrast, in the D102N mutant of the protease enzyme trypsin, the NH2, group of Asn-102 is hydrogen bonded to His-57 resulting in the inactive, tautomeric form and hence the loss of enzymatic activity. Although the, geometry of the catalytic triad in the PLA2 mutant remains the same as in, the WT, we were surprised that the conserved structural water, linking the, catalytic site with the ammonium group of Ala-1 of the interfacial site, was ejected by the proximity of the NH2 group of Asn-99. The NH2 group now, forms a direct hydrogen bond with the carbonyl group of Ala-1.
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<StructureSection load='1ceh' size='340' side='right'caption='[[1ceh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ceh]] 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=1CEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEH 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]] 1.9&#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></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=1ceh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ceh OCA], [https://pdbe.org/1ceh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ceh RCSB], [https://www.ebi.ac.uk/pdbsum/1ceh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ceh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PA21B_BOVIN PA21B_BOVIN] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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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/ce/1ceh_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=1ceh ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1CEH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CEH OCA].
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure and function of the catalytic site mutant Asp 99 Asn of phospholipase A2: absence of the conserved structural water., Kumar A, Sekharudu C, Ramakrishnan B, Dupureur CM, Zhu H, Tsai MD, Sundaralingam M, Protein Sci. 1994 Nov;3(11):2082-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7703854 7703854]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Phospholipase A(2)]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Dupureur CM]]
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[[Category: Dupureur, C.M.]]
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[[Category: Kumar A]]
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[[Category: Kumar, A.]]
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[[Category: Ramakrishnan B]]
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[[Category: Ramakrishnan, B.]]
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[[Category: Sekharudu C]]
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[[Category: Sekharudu, C.]]
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[[Category: Sundaralingam M]]
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[[Category: Sundaralingam, M.]]
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[[Category: Tsai M-D]]
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[[Category: Tsai, M.D.]]
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[[Category: Zhu H]]
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[[Category: Zhu, H.]]
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[[Category: CA]]
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[[Category: hydrolase (carboxylic ester)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:23:06 2007''
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Current revision

STRUCTURE AND FUNCTION OF THE CATALYTIC SITE MUTANT ASP99ASN OF PHOSPHOLIPASE A2: ABSENCE OF CONSERVED STRUCTURAL WATER

PDB ID 1ceh

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