SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold

被引：470

作者：

Martin, JL ^{[1
]}

McMillan, FM

机构：

[1] Univ Queensland, Ctr Drug Design & Dev, Inst Mol Biosci, Brisbane, Qld 4072, Australia

[2] Univ Queensland, Special Res Ctr Funct & Appl Genom, Inst Mol Biosci, Brisbane, Qld 4072, Australia

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2002年 / 12卷 / 06期

关键词：

D O I：

10.1016/S0959-440X(02)00391-3

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 S-adenosylmethionine-dependent methyltransferase enzymes share little sequence identity, but incorporate a highly conserved structural fold. Surprisingly, residues that bind the common cofactor are poorly conserved, although the binding site is localised to the same region of the fold. The substrate-binding region of the fold varies enormously. Over the past two years, there has been a significant increase in the number of structures that are known to incorporate this fold, including several uncharacterised proteins and two proteins that lack methyltransferase activity.

引用

页码：783 / 793

页数：11

共 60 条

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