1wvb

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[[Image:1wvb.gif|left|200px]]<br /><applet load="1wvb" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1wvb.gif|left|200px]]
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caption="1wvb, resolution 2.30&Aring;" />
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'''Crystal structure of human arginase I: the mutant E256Q'''<br />
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{{Structure
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|PDB= 1wvb |SIZE=350|CAPTION= <scene name='initialview01'>1wvb</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=S2C:S-2-(BORONOETHYL)-L-CYSTEINE'>S2C</scene>
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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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|GENE=
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}}
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'''Crystal structure of human arginase I: the mutant E256Q'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1WVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=S2C:'>S2C</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVB OCA].
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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].
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11278703 11278703]
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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]
[[Category: Arginase]]
[[Category: Arginase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: twinned crystal]]
[[Category: twinned crystal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:01:59 2008''

Revision as of 13:02, 20 March 2008

Image:1wvb.gif


PDB ID 1wvb

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: and
Activity: Arginase, with EC number 3.5.3.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human arginase I: the mutant E256Q


Overview

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

1WVB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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:11278703

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