3rla: Difference between revisions

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[[Image:3rla.gif|left|200px]]<br />
<applet load="3rla" size="450" color="white" frame="true" align="right" spinBox="true"
caption="3rla, resolution 2.54&Aring;" />
'''ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION'''<br />


==Overview==
==ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION==
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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9265637 (full description)]]
<StructureSection load='3rla' size='340' side='right'caption='[[3rla]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rla]] 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=3RLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RLA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rla OCA], [https://pdbe.org/3rla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rla RCSB], [https://www.ebi.ac.uk/pdbsum/3rla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rla ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARGI1_RAT ARGI1_RAT]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rl/3rla_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3rla ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
3RLA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with MN as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Sites: MNA, MNB and MNC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3RLA OCA]].
*[[Arginase 3D structures|Arginase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9265637 9265637]
[[Category: Large Structures]]
[[Category: Arginase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Christianson DW]]
[[Category: Christianson, D.W.]]
[[Category: Kanyo ZF]]
[[Category: Kanyo, Z.F.]]
[[Category: Scolnick LR]]
[[Category: Scolnick, L.R.]]
[[Category: MN]]
[[Category: arginine metabolism]]
[[Category: hydrolase]]
[[Category: urea cycle]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:46:42 2007''

Latest revision as of 09:43, 1 March 2024

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

3rla, resolution 2.54Å

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