1o76

From Proteopedia

Revision as of 12:00, 30 October 2007

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 ... [(full description)]

About this Structure

1O76 is a [Single protein] structure of sequence from [Pseudomonas putida] with CYN, K, HEM, CAM and TRS as [ligands]. Active as [Camphor 5-monooxygenase], with EC number [1.14.15.1]. Structure known Active Site: AC1. 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

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