1hqf: Difference between revisions

New page: left|200px<br /><applet load="1hqf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqf, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1hqf.jpg|left|200px]]<br /><applet load="1hqf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hqf.jpg|left|200px]]<br /><applet load="1hqf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hqf, resolution 2.9&Aring;" />
caption="1hqf, resolution 2.9&Aring;" />
'''CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH N-HYDROXY-L-ARGININE'''<br />
'''CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH N-HYDROXY-L-ARGININE'''<br />


==Overview==
==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.
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==
==About this Structure==
1HQF 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 and HAR 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HQF OCA].  
1HQF 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> and <scene name='pdbligand=HAR:'>HAR</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=1HQF OCA].  


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ash, D.E.]]
[[Category: Ash, D E.]]
[[Category: Cama, E.]]
[[Category: Cama, E.]]
[[Category: Christianson, D.W.]]
[[Category: Christianson, D W.]]
[[Category: Colleluori, D.M.]]
[[Category: Colleluori, D M.]]
[[Category: Cox, J.D.]]
[[Category: Cox, J D.]]
[[Category: HAR]]
[[Category: HAR]]
[[Category: MN]]
[[Category: MN]]
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[[Category: n-hydroxy-l-arginine (noha)]]
[[Category: n-hydroxy-l-arginine (noha)]]


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