1odo

From Proteopedia

Revision as of 13:46, 30 October 2007

1.85 A STRUCTURE OF CYP154A1 FROM STREPTOMYCES COELICOLOR A3(2)

Overview

The genus Streptomyces produces two-thirds of microbially derived, antibiotics. Polyketides form the largest and most diverse group of these, natural products. Antibiotic diversity of polyketides is generated during, their biosynthesis by several means, including postpolyketide modification, performed by oxidoreductases, a broad group of enzymes including, cytochrome P450 monooxygenases (CYPs). CYPs catalyze site-specific, oxidation of macrolide antibiotic precursors significantly affecting, antibiotic activity. Efficient manipulation of Streptomyces CYPs in, generating new antibiotics will require identification and/or engineering, of monooxygenases with activities toward a diverse array of chemical, substrates. To begin to link structure to function of CYPs involved in, secondary ... [(full description)]

About this Structure

1ODO is a [Single protein] structure of sequence from [Streptomyces coelicolor] with HEM and PIM as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Comparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways., Podust LM, Bach H, Kim Y, Lamb DC, Arase M, Sherman DH, Kelly SL, Waterman MR, Protein Sci. 2004 Jan;13(1):255-68. PMID:14691240

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