1hqg

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[[Image:1hqg.gif|left|200px]]<br /><applet load="1hqg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hqg.gif|left|200px]]
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caption="1hqg, resolution 2.&Aring;" />
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'''CRYSTAL STRUCTURE OF THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA'''<br />
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{{Structure
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|PDB= 1hqg |SIZE=350|CAPTION= <scene name='initialview01'>1hqg</scene>, resolution 2.&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ORN:ORNITHINE'>ORN</scene> and <scene name='pdbligand=URE:UREA'>URE</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 THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1HQG 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>, <scene name='pdbligand=ORN:'>ORN</scene> and <scene name='pdbligand=URE:'>URE</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=1HQG OCA].
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1HQG 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=1HQG OCA].
==Reference==
==Reference==
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Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase., Cox JD, Cama E, Colleluori DM, Pethe S, Boucher JL, Mansuy D, Ash DE, Christianson DW, Biochemistry. 2001 Mar 6;40(9):2689-701. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11258880 11258880]
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Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase., Cox JD, Cama E, Colleluori DM, Pethe S, Boucher JL, Mansuy D, Ash DE, Christianson DW, Biochemistry. 2001 Mar 6;40(9):2689-701. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11258880 11258880]
[[Category: Arginase]]
[[Category: Arginase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: product]]
[[Category: product]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:40:21 2008''

Revision as of 09:40, 20 March 2008

Image:1hqg.gif


PDB ID 1hqg

Drag the structure with the mouse to rotate
, resolution 2.Å
Ligands: , and
Activity: Arginase, with EC number 3.5.3.1
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA


Overview

Arginase is a binuclear Mn(2+) metalloenzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. X-ray crystal structures of arginase complexed to substrate analogues N(omega)-hydroxy-L-arginine and N(omega)-hydroxy-nor-L-arginine, as well as the products L-ornithine and urea, complete a set of structural "snapshots" along the reaction coordinate of arginase catalysis when interpreted along with the X-ray crystal structure of the arginase-transition-state analogue complex described in Kim et al. [Kim, N. N., Cox, J. D., Baggio, R. F., Emig, F. A., Mistry, S., Harper, S. L., Speicher, D. W., Morris, Jr., S. M., Ash, D. E., Traish, A. M., and Christianson, D. W. (2001) Biochemistry 40, 2678-2688]. Taken together, these structures render important insight on the structural determinants of tight binding inhibitors. Furthermore, we demonstrate for the first time the structural mechanistic link between arginase and NO synthase through their respective complexes with N(omega)-hydroxy-L-arginine. That N(omega)-hydroxy-L-arginine is a catalytic intermediate for NO synthase and an inhibitor of arginase reflects the reciprocal metabolic relationship between these two critical enzymes of L-arginine catabolism.

About this Structure

1HQG is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase., Cox JD, Cama E, Colleluori DM, Pethe S, Boucher JL, Mansuy D, Ash DE, Christianson DW, Biochemistry. 2001 Mar 6;40(9):2689-701. PMID:11258880

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