1o2e

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(New page: 200px<br /><applet load="1o2e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o2e, resolution 2.60&Aring;" /> '''Structure of the tri...)
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[[Image:1o2e.jpg|left|200px]]<br /><applet load="1o2e" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1o2e, resolution 2.60&Aring;" />
 
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'''Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2'''<br />
 
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==Overview==
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==Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2==
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Phospholipase A2 catalyses the hydrolysis of the ester bond of, 3-sn-phosphoglycerides. Here, we report the crystal structures of the free, and anisic acid-bound triple mutant (K53,56,120M) of bovine pancreatic, phospholipase A2. In the bound triple mutant structure, the small organic, molecule p-anisic acid is found in the active site, and one of the, carboxylate oxygen atoms is coordinated to the functionally important, primary calcium ion. The other carboxylate oxygen atom is hydrogen bonded, to the phenolic hydroxyl group of Tyr69. In addition, the bound anisic, acid molecule replaces one of the functionally important water molecules, in the active site. The residues 60-70, which are in a loop (surface, loop), are disordered in most of the bovine pancreatic phospholipase A2, structures. It is interesting to note that these residues are ordered in, the bound triple mutant structure but are disordered in the free triple, mutant structure. The organic crystallization ingredient, 2-methyl-2,4-pentanediol is found near the active site of the free triple, mutant structure. The overall tertiary folding and stereochemical, parameters for the final models of the free and anisic acid-bound triple, mutant are virtually identical.
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<StructureSection load='1o2e' size='340' side='right'caption='[[1o2e]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1o2e]] 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=1O2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O2E 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]] 2.6&#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=ANN:4-METHOXYBENZOIC+ACID'>ANN</scene>, <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=1o2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o2e OCA], [https://pdbe.org/1o2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o2e RCSB], [https://www.ebi.ac.uk/pdbsum/1o2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o2e 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/o2/1o2e_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=1o2e 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 A2 catalyses the hydrolysis of the ester bond of 3-sn-phosphoglycerides. Here, we report the crystal structures of the free and anisic acid-bound triple mutant (K53,56,120M) of bovine pancreatic phospholipase A2. In the bound triple mutant structure, the small organic molecule p-anisic acid is found in the active site, and one of the carboxylate oxygen atoms is coordinated to the functionally important primary calcium ion. The other carboxylate oxygen atom is hydrogen bonded to the phenolic hydroxyl group of Tyr69. In addition, the bound anisic acid molecule replaces one of the functionally important water molecules in the active site. The residues 60-70, which are in a loop (surface loop), are disordered in most of the bovine pancreatic phospholipase A2 structures. It is interesting to note that these residues are ordered in the bound triple mutant structure but are disordered in the free triple mutant structure. The organic crystallization ingredient 2-methyl-2,4-pentanediol is found near the active site of the free triple mutant structure. The overall tertiary folding and stereochemical parameters for the final models of the free and anisic acid-bound triple mutant are virtually identical.
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==About this Structure==
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Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2.,Sekar K, Vaijayanthi Mala S, Yogavel M, Velmurugan D, Poi MJ, Vishwanath BS, Gowda TV, Jeyaprakash AA, Tsai MD J Mol Biol. 2003 Oct 17;333(2):367-76. PMID:14529623<ref>PMID:14529623</ref>
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1O2E 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 and ANN as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1O2E OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2., Sekar K, Vaijayanthi Mala S, Yogavel M, Velmurugan D, Poi MJ, Vishwanath BS, Gowda TV, Jeyaprakash AA, Tsai MD, J Mol Biol. 2003 Oct 17;333(2):367-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14529623 14529623]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1o2e" style="background-color:#fffaf0;"></div>
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[[Category: Phospholipase A(2)]]
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[[Category: Single protein]]
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[[Category: Sekar, K.]]
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[[Category: Tsai, M.D.]]
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[[Category: Velmurugan, D.]]
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[[Category: ANN]]
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[[Category: CA]]
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[[Category: alpha helix]]
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[[Category: anisic acid]]
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[[Category: beta sheet]]
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[[Category: triple mutant]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:45:18 2007''
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Sekar K]]
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[[Category: Tsai MD]]
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[[Category: Velmurugan D]]

Current revision

Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2

PDB ID 1o2e

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