2cev

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(New page: 200px<br /><applet load="2cev" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cev, resolution 2.15&Aring;" /> '''ARGINASE FROM BACILL...)
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[[Image:2cev.jpg|left|200px]]<br /><applet load="2cev" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2cev, resolution 2.15&Aring;" />
 
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'''ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5'''<br />
 
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==Overview==
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==ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5==
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BACKGROUND: Arginase is a manganese-dependent enzyme that catalyzes the, hydrolysis of L-arginine to L-ornithine and urea. In ureotelic animals, arginase is the final enzyme of the urea cycle, but in many species it has, a wider role controlling the use of arginine for other metabolic purposes, including the production of creatine, polyamines, proline and nitric, oxide. Arginase activity is regulated by various small molecules, including the product L-ornithine. The aim of these structural studies was, to test aspects of the catalytic mechanism and to investigate the, structural basis of arginase inhibition. RESULTS: We report here the, crystal structures of arginase from Bacillus caldovelox at pH 5.6 and pH, 8.5, and of binary complexes of the enzyme with L-arginine, L-ornithine, and L-lysine at pH 8.5. The arginase monomer comprises a single compact, alpha/beta domain that further associates into a hexameric quaternary, structure. The binary complexes reveal a common mode of ligand binding, which places the substrate adjacent to the dimanganese centre. We also, observe a conformational change that impacts on the active site and is, coupled with the occupancy of an external site by guanidine or arginine., CONCLUSIONS: The structures reported here clarify aspects of the active, site and indicate key features of the catalytic mechanism, including, substrate coordination to one of the manganese ions and an orientational, role for a neighboring histidine residue. Stereospecificity for L-amino, acids is found to depend on their precise recognition at the active-site, rim. Identification of a second arginine-binding site, remote from the, active site, and associated conformational changes lead us to propose a, regulatory role for this site in substrate hydrolysis.
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<StructureSection load='2cev' size='340' side='right'caption='[[2cev]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cev]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_caldovelox Bacillus caldovelox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CEV 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]] 2.15&#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=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=2cev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cev OCA], [https://pdbe.org/2cev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cev RCSB], [https://www.ebi.ac.uk/pdbsum/2cev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cev ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARGI_BACCD ARGI_BACCD] Controls arginine catabolism.
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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/2cev_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=2cev 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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2CEV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_caldovelox Bacillus caldovelox] with MN and GAI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CEV OCA].
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*[[Arginase 3D structures|Arginase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily., Bewley MC, Jeffrey PD, Patchett ML, Kanyo ZF, Baker EN, Structure. 1999 Apr 15;7(4):435-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10196128 10196128]
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[[Category: Large Structures]]
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[[Category: Arginase]]
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[[Category: Baker EN]]
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[[Category: Bacillus caldovelox]]
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[[Category: Bewley MC]]
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[[Category: Single protein]]
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[[Category: Jeffrey PD]]
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[[Category: Baker, E.N.]]
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[[Category: Kanyo ZF]]
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[[Category: Bewley, M.C.]]
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[[Category: Patchett ML]]
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[[Category: Jeffrey, P.D.]]
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[[Category: Kanyo, Z.F.]]
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[[Category: Patchett, M.L.]]
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[[Category: GAI]]
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[[Category: MN]]
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[[Category: arginine hydrolysis]]
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[[Category: enzyme]]
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[[Category: hydrolase]]
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[[Category: manganese metalloenzyme]]
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[[Category: nitrogen metabolism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:06:10 2007''
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Current revision

ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5

PDB ID 2cev

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