1O76

CYANIDE COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA

Summary for 1O76

• Entry DOI: 10.2210/pdb1o76/pdb
• Related: 1AKD 1C8J 1CP4 1DZ4 1DZ6 1DZ8 1DZ9 1GEB 1GEK 1GEM 1GJM 1IWI 1IWJ 1IWK 1J51 1K2O 1MPW 1NOO 1PHA 1PHB 1PHC 1PHD 1PHE 1PHF 1PHG 1QMQ 2CP4 2CPP 3CP4 3CPP 4CP4 4CPP 5CP4 5CPP 6CP4 6CPP 7CPP 8CPP
• Descriptor: CYTOCHROME P450-CAM, PROTOPORPHYRIN IX CONTAINING FE, CYANIDE ION, ... (7 entities in total)
• Functional Keywords: oxidoreductase, mono-oxygenase, heme, electron transport
• Biological source: PSEUDOMONAS PUTIDA
• Total number of polymer chains: 2
• Total formula weight: 95004.70

Authors

Fedorov, R.,Ghosh, D.,Schlichting, I. (deposition date: 2002-10-23, release date: 2002-12-19, Last modification date: 2024-05-08)

Primary citation

Fedorov, R.,Ghosh, D.,Schlichting, I.
Crystal Structures of Cyanide Complexes of P450Cam and the Oxygenase Domain of Inducible Nitric Oxide Synthase-Structural Models of the Short-Lived Oxygen Complexes
Arch.Biochem.Biophys., 409:25-, 2003

PubMed Abstract: 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.

PubMed: 12464241
DOI: 10.1016/S0003-9861(02)00555-6

Experimental method

X-RAY DIFFRACTION (1.8 Å)