The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase

被引：54
作者：
Schubert, HL
Wilson, KS [1 ]
Raux, E
Woodcock, SC
Warren, MJ
机构：
[1] Univ York, Dept Chem, Prot Struct Grp, York YO1 5DD, N Yorkshire, England
[2] UCL, Inst Ophthalmol, Dept Mol Genet, London EC1V 9EL, England
来源：
NATURE STRUCTURAL BIOLOGY | 1998年 / 5卷 / 07期
基金：
英国惠康基金;
关键词：
D O I：
10.1038/846
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：
Biosynthesis of the corrin ring of vitamin B-12 requires the action of six S-adenosyl-L-methionine (AdoMet) dependent transmethylases, closely related in sequence. The first X-ray structure of one of these, cobalt-precorrin-4 transmethylase, CbiF, from Bacillus megaterium has been determined to a resolution of 2.4 Angstrom. CbiF contains two alpha/beta domains forming a trough in which S-adenosyl-L-homocysteine (AdoHcy) binds. The location of AdoHcy and a number of conserved residues, helps define the precorrin binding site. A second crystal form determined at 3.1 Angstrom resolution highlights the flexibility of two loops around this site. CbiF employs a unique mode of AdoHcy binding and represents a new class of transmethylase.
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收藏
页码：585 / 592
页数：8
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