4rla

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[[Image:4rla.gif|left|200px]]
 
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{{Structure
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==ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION==
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|PDB= 4rla |SIZE=350|CAPTION= <scene name='initialview01'>4rla</scene>, resolution 2.94&Aring;
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<StructureSection load='4rla' size='340' side='right'caption='[[4rla]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
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|SITE= <scene name='pdbsite=MNA:Bi-Mn+Nuclear+Binding+Site'>MNA</scene>, <scene name='pdbsite=MNB:Bi-Mn+Nuclear+Binding+Site'>MNB</scene> and <scene name='pdbsite=MNC:Bi-Mn+Nuclear+Binding+Site'>MNC</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
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<table><tr><td colspan='2'>[[4rla]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RLA FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.94&#8491;</td></tr>
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|GENE= PARGR-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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}}
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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=4rla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rla OCA], [https://pdbe.org/4rla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rla RCSB], [https://www.ebi.ac.uk/pdbsum/4rla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rla ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARGI1_RAT ARGI1_RAT]
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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/rl/4rla_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=4rla ConSurf].
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<div style="clear:both"></div>
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'''ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION'''
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==See Also==
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*[[Arginase 3D structures|Arginase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Arginase is a thermostable (Tm = 75 degrees C) binuclear manganese metalloenzyme which hydrolyzes l-arginine to form l-ornithine and urea. The three-dimensional structures of native metal-depleted arginase, metal-loaded H101N arginase, and metal-depleted H101N arginase have been determined by X-ray crystallographic methods to probe the roles of the manganese ion in site A (Mn2+A) and its ligand H101 in catalysis and thermostability. We correlate these structures with thermal stability and catalytic activity measurements reported here and elsewhere [Cavalli, R. C., Burke, C. J., Kawamoto, S., Soprano, D. R., and Ash, D. E. (1994) Biochemistry 33, 10652-10657]. We conclude that the substitution of a wild-type histidine ligand to Mn2+A compromises metal binding, which in turn compromises protein thermostability and catalytic function. Therefore, a fully occupied binuclear manganese metal cluster is required for optimal catalysis and thermostability.
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[[Category: Large Structures]]
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==About this Structure==
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4RLA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RLA OCA].
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==Reference==
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Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function., Scolnick LR, Kanyo ZF, Cavalli RC, Ash DE, Christianson DW, Biochemistry. 1997 Aug 26;36(34):10558-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9265637 9265637]
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[[Category: Arginase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Christianson DW]]
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[[Category: Christianson, D W.]]
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[[Category: Kanyo ZF]]
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[[Category: Kanyo, Z F.]]
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[[Category: Scolnick LR]]
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[[Category: Scolnick, L R.]]
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[[Category: MN]]
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[[Category: arginine metabolism]]
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[[Category: hydrolase]]
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[[Category: urea cycle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:50 2008''
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Current revision

ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION

PDB ID 4rla

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