PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF AN ENZYME INVOLVED IN ERYTHROMYCIN BIOSYNTHESIS - CYTOCHROME P450ERYF

被引:41
作者
CUPPVICKERY, JR
LI, HY
POULOS, TL
机构
[1] UNIV CALIF IRVINE, DEPT PHYSIOL & BIOPHYS, IRVINE, CA 92717 USA
[2] UNIV CALIF IRVINE, DEPT MOLEC BIOL & BIOCHEM, IRVINE, CA 92717 USA
关键词
CYTOCHROME P450; ERYTHROMYCIN; P450ERYF; CRYSTALLIZATION;
D O I
10.1002/prot.340200210
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cytochrome P450eryF was overexpressed in Escherichia coli and purified in high yield. Crystals of the protein in the presence of the substrate, 6-deoxyerythronolide B, have been obtained by the hanging drop vapor diffusion method, using polyethylene glycol 4000 as a precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of a = 54.16 Angstrom, b = 79.67 Angstrom, and c = 99.48 Angstrom and one molecule per asymmetric unit. A complete native data set has been collected to a resolution of 2.1 Angstrom, and anomalous dispersion difference Patterson maps have revealed the location of the single heme iron atom. (C) 1994 Wiley-Liss, Inc.
引用
收藏
页码:197 / 201
页数:5
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