1wvb

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{{STRUCTURE_1wvb| PDB=1wvb | SCENE= }}
{{STRUCTURE_1wvb| PDB=1wvb | SCENE= }}
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'''Crystal structure of human arginase I: the mutant E256Q'''
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===Crystal structure of human arginase I: the mutant E256Q===
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==Overview==
 
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The structure of the trimeric, manganese metalloenzyme, rat liver arginase, has been previously determined at 2.1-A resolution (Kanyo, Z. F., Scolnick, L. R., Ash, D. E., and Christianson, D. W., (1996) Nature 383, 554-557). A key feature of this structure is a novel S-shaped oligomerization motif at the carboxyl terminus of the protein that mediates approximately 54% of the intermonomer contacts. Arg-308, located within this oligomerization motif, nucleates a series of intramonomer and intermonomer salt links. In contrast to the trimeric wild-type enzyme, the R308A, R308E, and R308K variants of arginase exist as monomeric species, as determined by gel filtration and analytical ultracentrifugation, indicating that mutation of Arg-308 shifts the equilibrium for trimer dissociation by at least a factor of 10(5). These monomeric arginase variants are catalytically active, with k(cat)/K(m) values that are 13-17% of the value for wild-type enzyme. The arginase variants are characterized by decreased temperature stability relative to the wild-type enzyme. Differential scanning calorimetry shows that the midpoint temperature for unfolding of the Arg-308 variants is in the range of 63.6-65.5 degrees C, while the corresponding value for the wild-type enzyme is 70 degrees C. The three-dimensional structure of the R308K variant has been determined at 3-A resolution. At the high protein concentrations utilized in the crystallizations, this variant exists as a trimer, but weakened salt link interactions are observed for Lys-308.
 
==About this Structure==
==About this Structure==
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1WVB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVB OCA].
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1WVB is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVB OCA].
==Reference==
==Reference==
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Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid., Lavulo LT, Sossong TM Jr, Brigham-Burke MR, Doyle ML, Cox JD, Christianson DW, Ash DE, J Biol Chem. 2001 Apr 27;276(17):14242-8. Epub 2001 Jan 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11278703 11278703]
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<ref group="xtra">PMID:11278703</ref><references group="xtra"/>
[[Category: Arginase]]
[[Category: Arginase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
 
[[Category: Centeno, F.]]
[[Category: Centeno, F.]]
[[Category: Christianson, D W.]]
[[Category: Christianson, D W.]]
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[[Category: Mutant e256q]]
[[Category: Mutant e256q]]
[[Category: Twinned crystal]]
[[Category: Twinned crystal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:11:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:10:56 2009''

Revision as of 10:10, 17 February 2009

Template:STRUCTURE 1wvb

Crystal structure of human arginase I: the mutant E256Q

About this Structure

1WVB is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Lavulo LT, Sossong TM Jr, Brigham-Burke MR, Doyle ML, Cox JD, Christianson DW, Ash DE. Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid. J Biol Chem. 2001 Apr 27;276(17):14242-8. Epub 2001 Jan 24. PMID:11278703 doi:10.1074/jbc.M010575200

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