1g4i

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(New page: 200px<br /><applet load="1g4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4i, resolution 0.97&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1g4i.jpg|left|200px]]<br /><applet load="1g4i" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1g4i, resolution 0.97&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE BOVINE PANCREATIC PHOSPHOLIPASE A2 AT 0.97A'''<br />
 
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==Overview==
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==Crystal structure of the bovine pancreatic phospholipase A2 at 0.97A==
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Using synchrotron radiation and a CCD camera, X-ray data have been, collected from wild-type bovine pancreatic phospholipase A(2) at 100 K to, 0.97 A resolution allowing full anisotropic refinement. The final model, has a conventional R factor of 9.44% for all reflections, with a mean, standard uncertainty for the positional parameters of 0.031 A as, calculated from inversion of the full positional least-squares matrix. At, 0.97 A resolution, bovine pancreatic phospholipase A(2) reveals for the, first time that its rigid scaffolding does not preclude flexibility, which, probably plays an important role in the catalytic process. Functionally, important regions (the interfacial binding site and calcium-binding loop), are located at the molecular surface, where conformational variability is, more pronounced. A cluster of 2-methyl-2,4-pentanediol molecules is, present at the entrance of the hydrophobic channel that leads to the, catalytic site and mimics the fatty-acid chains of a substrate analogue., Bovine pancreatic phospholipase A(2) at atomic resolution is compared with, previous crystallographic structures and with models derived from nuclear, magnetic resonance studies. Given the high structural similarity among, extracellular phospholipases A(2) observed so far at lower resolution, the, results arising from this structural analysis are expected to be of, general validity for this class of enzymes.
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<StructureSection load='1g4i' size='340' side='right'caption='[[1g4i]], [[Resolution|resolution]] 0.97&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1g4i]] 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=1G4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G4I 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]] 0.97&#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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=1g4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g4i OCA], [https://pdbe.org/1g4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g4i RCSB], [https://www.ebi.ac.uk/pdbsum/1g4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g4i 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/g4/1g4i_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=1g4i 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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Using synchrotron radiation and a CCD camera, X-ray data have been collected from wild-type bovine pancreatic phospholipase A(2) at 100 K to 0.97 A resolution allowing full anisotropic refinement. The final model has a conventional R factor of 9.44% for all reflections, with a mean standard uncertainty for the positional parameters of 0.031 A as calculated from inversion of the full positional least-squares matrix. At 0.97 A resolution, bovine pancreatic phospholipase A(2) reveals for the first time that its rigid scaffolding does not preclude flexibility, which probably plays an important role in the catalytic process. Functionally important regions (the interfacial binding site and calcium-binding loop) are located at the molecular surface, where conformational variability is more pronounced. A cluster of 2-methyl-2,4-pentanediol molecules is present at the entrance of the hydrophobic channel that leads to the catalytic site and mimics the fatty-acid chains of a substrate analogue. Bovine pancreatic phospholipase A(2) at atomic resolution is compared with previous crystallographic structures and with models derived from nuclear magnetic resonance studies. Given the high structural similarity among extracellular phospholipases A(2) observed so far at lower resolution, the results arising from this structural analysis are expected to be of general validity for this class of enzymes.
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==About this Structure==
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X-ray structure of bovine pancreatic phospholipase A2 at atomic resolution.,Steiner RA, Rozeboom HJ, de Vries A, Kalk KH, Murshudov GN, Wilson KS, Dijkstra BW Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):516-26. PMID:11264580<ref>PMID:11264580</ref>
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1G4I 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, CL, MRD and MPD 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=1G4I 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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X-ray structure of bovine pancreatic phospholipase A2 at atomic resolution., Steiner RA, Rozeboom HJ, de Vries A, Kalk KH, Murshudov GN, Wilson KS, Dijkstra BW, Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):516-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11264580 11264580]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1g4i" 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: Dijkstra, B.W.]]
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[[Category: Kalk, K.H.]]
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[[Category: Murshudov, G.N.]]
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[[Category: Rozeboom, H.J.]]
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[[Category: Steiner, R.A.]]
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[[Category: Vries, A.de.]]
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[[Category: Wilson, K.S.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: MPD]]
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[[Category: MRD]]
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[[Category: lipid degradation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:41:55 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: Dijkstra BW]]
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[[Category: Kalk KH]]
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[[Category: Murshudov GN]]
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[[Category: Rozeboom HJ]]
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[[Category: Steiner RA]]
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[[Category: Wilson KS]]
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[[Category: De Vries A]]

Current revision

Crystal structure of the bovine pancreatic phospholipase A2 at 0.97A

PDB ID 1g4i

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