The three-dimensional structure of shikimate kinase

被引:75
作者
Krell, T
Coggins, JR
Lapthorn, AJ [1 ]
机构
[1] Univ Glasgow, Inst Biol & Life Sci, Dept Chem, Glasgow G12 8QQ, Lanark, Scotland
[2] Univ Glasgow, Inst Biol & Life Sci, Div Biochem & Mol Biol, Glasgow G12 8QQ, Lanark, Scotland
基金
英国生物技术与生命科学研究理事会;
关键词
shikimate kinase; X-ray analysis; phosphoryl transfer; shikimate pathway; drug design;
D O I
10.1006/jmbi.1998.1755
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
The three-dimensional structure of shikimate kinase from Erwinia chrysanthemi has been determined by multiple isomorphous replacement. Two models are presented: a high resolution 1.9 Angstrom model and a 2.6 Angstrom model which contains bound Mg-ADP. The enzyme is an alpha/beta protein consisting of a central sheet of five parallel beta-strands flanked by alpha-helices with overall topology similar to adenylate kinase. Evidence is presented that shikimate kinase undergoes major conformational changes on ligand binding. It resembles adenylate kinase in having a P-loop containing core structure and two flexible domains which undergo induced fit movement on substrate binding. The binding of Mg(2+) in the active site of shikimate kinase involves direct interaction with two protein side-chains which is different from the situation found in adenylate kinase. Shikimate kinase has a readily identifiable Walker A-motif and a recognisable but modified Walker B-motif. Comparison of shikimate kinase to adenylate kinase has led to the identification of an adenine-binding motif (I/VDAXQ/NXP). Difference Fourier calculations have revealed the shikimate binding site which corresponds to the location of the AMP-binding site in adenylate kinase. A model for shikimate-binding is presented. (C) 1998 Academic Press Limited.
引用
收藏
页码:983 / 997
页数:15
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