1o76
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of the ternary cyanide complex of P450cam and | + | The crystal structure of the ternary cyanide complex of P450cam and camphor was determined to 1.8A resolution and found to be identical with the structure of the active oxygen complex [I. Schlichting et al., 2000, Science 287, 1615]. Notably, cyanide binds in a bent mode and induces the active conformation that is characterized by the presence of two water molecules and a flip of the carbonyl of the conserved Asp251. The structure of the ternary complex of cyanide, L-arginine, and the oxygenase domain of inducible nitric oxide synthase was determined to 2.4A resolution. Cyanide binds essentially linearly, interacts with L-Arg, and induces the binding of a water molecule at the active site. This water is positioned by backbone interactions, located 2.8A from the nitrogen atom of cyanide, and could provide a proton required for O-O bond scission in the hydroxylation reaction of nitric oxide synthase. |
==About this Structure== | ==About this Structure== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:09 2008'' |
Revision as of 12:14, 21 February 2008
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CYANIDE COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA
Overview
The crystal structure of the ternary cyanide complex of P450cam and camphor was determined to 1.8A resolution and found to be identical with the structure of the active oxygen complex [I. Schlichting et al., 2000, Science 287, 1615]. Notably, cyanide binds in a bent mode and induces the active conformation that is characterized by the presence of two water molecules and a flip of the carbonyl of the conserved Asp251. The structure of the ternary complex of cyanide, L-arginine, and the oxygenase domain of inducible nitric oxide synthase was determined to 2.4A resolution. Cyanide binds essentially linearly, interacts with L-Arg, and induces the binding of a water molecule at the active site. This water is positioned by backbone interactions, located 2.8A from the nitrogen atom of cyanide, and could provide a proton required for O-O bond scission in the hydroxylation reaction of nitric oxide synthase.
About this Structure
1O76 is a Single protein structure of sequence from Pseudomonas putida with , , , and as ligands. Active as Camphor 5-monooxygenase, with EC number 1.14.15.1 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes., Fedorov R, Ghosh DK, Schlichting I, Arch Biochem Biophys. 2003 Jan 1;409(1):25-31. PMID:12464241
Page seeded by OCA on Thu Feb 21 14:14:09 2008
Categories: Camphor 5-monooxygenase | Pseudomonas putida | Single protein | Fedorov, R. | Ghosh, D. | Schlichting, I. | CAM | CYN | HEM | K | TRS | Electron transport | Heme | Mono-oxygenase | Oxidoreductase
