CRYSTAL-STRUCTURE OF THE HHAL DNA METHYLTRANSFERASE COMPLEXED WITH S-ADENOSYL-L-METHIONINE

被引：362

作者：

CHENG, XD ^{[1
]}

KUMAR, S ^{[1
]}

POSFAI, J ^{[1
]}

PFLUGRATH, JW ^{[1
]}

ROBERTS, RJ ^{[1
]}

机构：

[1] NEW ENGLAND BIOLABS INC,BEVERLY,MA 01915

来源：

CELL | 1993年 / 74卷 / 02期

关键词：

D O I：

10.1016/0092-8674(93)90421-L

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 first three-dimensional structure of a DNA methyltransferase is presented. The crystal structure of the DNA (cytosine-5)-methyltransferase, M.Hhal (recognition sequence: GCGC), complexed with S-adenosyl-L-methionine has been determined and refined at 2.5 angstrom resolution. The core of the structure is dominated by sequence motifs conserved among all DNA (cytosine-5)-methyltransferases, and these are responsible for cofactor binding and methyltransferase function.

引用

页码：299 / 307

页数：9

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