1h70
From Proteopedia
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- | [[Image:1h70. | + | [[Image:1h70.jpg|left|200px]]<br /><applet load="1h70" size="450" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1h70" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1h70, resolution 1.80Å" /> | caption="1h70, resolution 1.80Å" /> | ||
'''DDAH FROM PSEUDOMONAS AERUGINOSA. C249S MUTANT COMPLEXED WITH CITRULLINE'''<br /> | '''DDAH FROM PSEUDOMONAS AERUGINOSA. C249S MUTANT COMPLEXED WITH CITRULLINE'''<br /> | ||
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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/Dimethylargininase Dimethylargininase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.18 3.5.3.18] | + | 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] Known structural/functional Site: <scene name='pdbsite=CIR:Cir Binding Site For Chain A'>CIR</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H70 OCA]. |
==Reference== | ==Reference== | ||
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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 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:04:29 2007'' |
Revision as of 13:54, 18 December 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 substrate that effectively maintains the orientation of, the scissile bond of the substrate with respect to the catalytic residues., The DDAH structure will form a basis for the rational design of selective, inhibitors, which are of potential use in modulating NO synthase activity, in pathological settings.
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 Known structural/functional Site: . 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
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