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1ceh

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[[Image:1ceh.gif|left|200px]]
 
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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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The line below this paragraph, containing "STRUCTURE_1ceh", creates the "Structure Box" on the page.
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<StructureSection load='1ceh' size='340' side='right'caption='[[1ceh]], [[Resolution|resolution]] 1.90&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'>[[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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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]] 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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{{STRUCTURE_1ceh| PDB=1ceh | SCENE= }}
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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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'''STRUCTURE AND FUNCTION OF THE CATALYTIC SITE MUTANT ASP99ASN OF PHOSPHOLIPASE A2: ABSENCE OF CONSERVED STRUCTURAL WATER'''
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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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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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==About this Structure==
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1CEH 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=1CEH OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/7703854 7703854]
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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: Dupureur, C M.]]
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[[Category: Dupureur CM]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:38:32 2008''
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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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