2zp3

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[[Image:2zp3.png|left|200px]]
 
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==Carboxylic ester hydrolase, single mutant d49n of bovine pancreatic pla2 enzyme==
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The line below this paragraph, containing "STRUCTURE_2zp3", creates the "Structure Box" on the page.
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<StructureSection load='2zp3' size='340' side='right'caption='[[2zp3]], [[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'>[[2zp3]] 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=2ZP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZP3 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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_2zp3| PDB=2zp3 | 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=2zp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zp3 OCA], [https://pdbe.org/2zp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zp3 RCSB], [https://www.ebi.ac.uk/pdbsum/2zp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zp3 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/zp/2zp3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2zp3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phospholipase A(2) hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad (Asp99 and His48) along with a nucleophilic water molecule is responsible for enzyme hydrolysis. Furthermore, the residue Asp49 in the calcium-binding loop is essential for controlling the binding of the calcium ion and the catalytic action of phospholipase A(2). To elucidate the structural role of His48 and Asp49, the crystal structures of three active-site single mutants H48N, D49N and D49K have been determined at 1.9 A resolution. Although the catalytically important calcium ion is present in the H48N mutant, the crystal structure shows that proton transfer is not possible from the catalytic water to the mutated residue. In the case of the Asp49 mutants, no calcium ion was found in the active site. However, the tertiary structures of the three active-site mutants are similar to that of the trigonal recombinant enzyme. Molecular-dynamics simulation studies provide a good explanation for the crystallographic results.
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===Carboxylic ester hydrolase, single mutant d49n of bovine pancreatic pla2 enzyme===
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Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A(2).,Kanaujia SP, Sekar K Acta Crystallogr D Biol Crystallogr. 2008 Oct;64(Pt 10):1003-11. Epub 2008, Sep 19. PMID:18931407<ref>PMID:18931407</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_18931407}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2zp3" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18931407 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18931407}}
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==About this Structure==
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[[2zp3]] is a 1 chain structure of [[Phospholipase A2]] with 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=2ZP3 OCA].
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==See Also==
==See Also==
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*[[Phospholipase A2]]
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:18931407</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Kanaujia, S P.]]
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[[Category: Large Structures]]
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[[Category: Sekar, K.]]
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[[Category: Kanaujia SP]]
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[[Category: Active site mutant]]
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[[Category: Sekar K]]
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[[Category: Calcium]]
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[[Category: Hydrolase]]
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[[Category: Lipid degradation]]
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[[Category: Metal binding protein]]
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[[Category: Metal-binding]]
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[[Category: Pyrrolidone carboxylic acid]]
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[[Category: Secreted]]
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Current revision

Carboxylic ester hydrolase, single mutant d49n of bovine pancreatic pla2 enzyme

PDB ID 2zp3

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