Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centred rearrangements

被引：139
作者：
Zhang, ZH
Ren, JS
Harlos, K
McKinnon, CH
Clifton, IJ
Schofield, CJ
机构：
[1] Oxford Ctr Mol Sci, Oxford OX1 3QY, England
[2] Dyson Perrins Lab, Dept Chem, Oxford OX1 3QY, England
[3] Wellcome Trust Ctr Human Genet, Struct Biol Div, Oxford OX3 7BN, England
[4] Oxford Ctr Mol Sci, Oxford OX3 7BN, England
来源：
FEBS LETTERS | 2002年 / 517卷 / 1-3期
基金：
英国生物技术与生命科学研究理事会; 英国惠康基金; 英国医学研究理事会; 英国工程与自然科学研究理事会;
关键词：
clavaminate synthase; clavulanic acid; dioxygenase; non-haem; 2-oxoglutarate; oxygenase;
D O I：
10.1016/S0014-5793(02)02520-6
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：
Clavaminate synthase (CAS), a 2-oxoglutarate (2OG) dependent dioxygenase, catalyses three steps in the biosynthesis of clavulanic acid. Crystals of CAS complexed with Fe(II), 2OG and deoxyguanidinoproclavaminate were exposed to nitric oxide (NO) acting as a dioxygen analogue. Prior to exposure with NO, the active site Fe(II) is octahedrally coordinated by a water molecule, the 2-oxo and 1-carboxylate groups of 2OG, and the side-chains of an aspartyl and two histidinyl residues. NO binds to the position previously occupied by the 2OG 1-carboxylate concomitant with rearrangement of the latter to the position previously occupied by the displaced water. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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页码：7 / 12
页数：6
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