CRYSTAL-STRUCTURE OF AN N-TERMINAL FRAGMENT OF THE DNA GYRASE B-PROTEIN

被引:502
作者
WIGLEY, DB [1 ]
DAVIES, GJ [1 ]
DODSON, EJ [1 ]
MAXWELL, A [1 ]
DODSON, G [1 ]
机构
[1] UNIV LEICESTER,DEPT BIOCHEM,LEICESTER LE1 7RH,ENGLAND
基金
英国惠康基金;
关键词
D O I
10.1038/351624a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, complexed with a nonhydrolysable ATP analogue, has been solved at 2.5 angstrom resolution. It consists of two domains, both containing novel protein folds. The protein fragment forms a dimer, whose N-terminal domains are responsible for ATP binding and hydrolysis. The C-terminal domains form the sides of a 20 angstrom hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction.
引用
收藏
页码:624 / 629
页数:6
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