4rla
From Proteopedia
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| - | [[Image:4rla.gif|left|200px]]<br /><applet load="4rla" size=" | + | [[Image:4rla.gif|left|200px]]<br /><applet load="4rla" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="4rla, resolution 2.94Å" /> | caption="4rla, resolution 2.94Å" /> | ||
'''ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION'''<br /> | '''ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 4RLA 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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http:// | + | 4RLA 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 <scene name='pdbligand=MN:'>MN</scene> 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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RLA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: urea cycle]] | [[Category: urea cycle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:53:09 2008'' |
Revision as of 08:53, 3 February 2008
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ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION
Overview
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.
About this Structure
4RLA is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Arginase, with EC number 3.5.3.1 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
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:9265637
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