CRYSTAL-STRUCTURE OF TRICHOSANTHIN-NADPH COMPLEX AT 1.7 ANGSTROM RESOLUTION REVEALS ACTIVE-SITE ARCHITECTURE

被引:47
|
作者
XIONG, JP [1 ]
XIA, ZX [1 ]
WANG, Y [1 ]
机构
[1] CHINESE ACAD SCI,SHANGHAI INST ORGAN CHEM,SHANGHAI 200032,PEOPLES R CHINA
来源
NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 10期
关键词
D O I
10.1038/nsb1094-695
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
We describe here the crystal structure of the trichosanthin-NADPH complex determined at a resolution of 1.7 Angstrom. The adenine base stacks between Tyr 70 and Tyr 111. Aug 163, Glu 160 and Tyr 70 form hydrogen bonds to N(3), O(3') and, through a water molecule, to N(9) of adenosine, respectively. This is the first high resolution structure of a complex between a ribosome-inactivating protein and a substrate analogue, in which the electron density of the IV-glycosidic bond is well defined and the preassociated water, thought to be responsible for hydrolyzing the N-C bond, is also explicitly elucidated.
引用
收藏
页码:695 / 700
页数:6
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