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.
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页码：299 / 307
页数：9
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