1h70: Difference between revisions
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|SITE= <scene name='pdbsite=CIR:Cir+Binding+Site+For+Chain+A'>CIR</scene> | |SITE= <scene name='pdbsite=CIR:Cir+Binding+Site+For+Chain+A'>CIR</scene> | ||
|LIGAND= <scene name='pdbligand=CIR:CITRULLINE'>CIR</scene> | |LIGAND= <scene name='pdbligand=CIR:CITRULLINE'>CIR</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h70 OCA], [http://www.ebi.ac.uk/pdbsum/1h70 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h70 RCSB]</span> | |||
}} | }} | ||
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[[Category: Tilley, S.]] | [[Category: Tilley, S.]] | ||
[[Category: Vallance, P.]] | [[Category: Vallance, P.]] | ||
[[Category: ddah]] | [[Category: ddah]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: nitric oxide synthase inhibitor]] | [[Category: nitric oxide synthase inhibitor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:59:07 2008'' | ||
Revision as of 17:59, 30 March 2008
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| 1h70, resolution 1.80Å | |||||||||||||
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| Sites: | CIR | ||||||||||||
| Ligands: | CIR | ||||||||||||
| Activity: | Dimethylargininase, with EC number 3.5.3.18 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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