1h70
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1H70 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]] with CIR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1H70 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]] with CIR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Dimethylargininase Dimethylargininase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.18 3.5.3.18]]. Structure known Active Site: CIR. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H70 OCA]]. |
==Reference== | ==Reference== | ||
Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase., Murray-Rust J, Leiper J, McAlister M, Phelan J, Tilley S, Santa Maria J, Vallance P, McDonald N, Nat Struct Biol. 2001 Aug;8(8):679-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11473257 11473257] | Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase., Murray-Rust J, Leiper J, McAlister M, Phelan J, Tilley S, Santa Maria J, Vallance P, McDonald N, Nat Struct Biol. 2001 Aug;8(8):679-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11473257 11473257] | ||
| + | [[Category: Dimethylargininase]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nitric oxide synthase inhibitor]] | [[Category: nitric oxide synthase inhibitor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:29:25 2007'' |
Revision as of 08:24, 30 October 2007
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DDAH FROM PSEUDOMONAS AERUGINOSA. C249S MUTANT COMPLEXED WITH CITRULLINE
Overview
Nitric oxide synthase is inhibited by asymmetric NG-methylated derivatives, of arginine whose cellular levels are controlled in part by, dimethylarginine dimethylaminohydrolase (DDAH, EC 3.5.3.18). Levels of, asymmetric NG,NG-dimethylarginine (ADMA) are known to correlate with, certain disease states. Here, the first structure of a DDAH shows an, unexpected similarity to arginine:glycine amidinotransferase (EC 2.1.4.1), and arginine deiminase (EC 3.5.3.6), thus defining a superfamily of, arginine-modifying enzymes. The identification of a Cys-His-Glu catalytic, triad and the structures of a Cys to Ser point mutant bound to both, substrate and product suggest a reaction mechanism. Comparison of the, ADMA-DDAH and arginine-amidinotransferase complexes reveals a dramatic, rotation of the ... [(full description)]
About this Structure
1H70 is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with CIR as [ligand]. Active as [Dimethylargininase], with EC number [3.5.3.18]. Structure known Active Site: CIR. Full crystallographic information is available from [OCA].
Reference
Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase., Murray-Rust J, Leiper J, McAlister M, Phelan J, Tilley S, Santa Maria J, Vallance P, McDonald N, Nat Struct Biol. 2001 Aug;8(8):679-83. PMID:11473257
Page seeded by OCA on Tue Oct 30 10:29:25 2007
