2bvj

From Proteopedia

Revision as of 10:57, 30 October 2007

LIGAND-FREE STRUCTURE OF CYTOCHROME P450 PIKC (CYP107L1)

Overview

The pikromycin (Pik)/methymycin biosynthetic pathway of Streptomyces, venezuelae represents a valuable system for dissecting the fundamental, mechanisms of modular polyketide biosynthesis, aminodeoxysugar assembly, glycosyltransfer, and hydroxylation leading to the production of a series, of macrolide antibiotics, including the natural ketolides narbomycin and, pikromycin. In this study, we describe four x-ray crystal structures and, allied functional studies for PikC, the remarkable P450 monooxygenase, responsible for production of a number of related macrolide products from, the Pik pathway. The results provide important new insights into the, structural basis for the C10/C12 and C12/C14 hydroxylation patterns for, the 12-(YC-17) and 14-membered ring (narbomycin) macrolides, ... [(full description)]

About this Structure

2BVJ is a [Single protein] structure of sequence from [Streptomyces venezuelae] with HEM, BME and DTT as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae., Sherman DH, Li S, Yermalitskaya LV, Kim Y, Smith JA, Waterman MR, Podust LM, J Biol Chem. 2006 Sep 8;281(36):26289-97. Epub 2006 Jul 6. PMID:16825192

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