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学科主题: 生命有机化学
题名: Crystal structures of the complexes of trichosanthin with four substrate analogs and catalytic mechanism of RNA N-Glycosidase
其他题名: 天花粉蛋白与四种底物类似物的复合物的晶体结构及RNA N-糖苷酶的催化机理
作者: Gu YJ(顾亦军) ; Xia ZX(夏宗芗)
通讯作者: 夏宗芗
刊名: Proteins: St
发表日期: 2000
卷: Funct., Genet. 2000, 39, 期:1, 页:37-46
收录类别: SCI
部门归属: 中国科学院上海有机化学研究所生命有机国家开放实验室
英文摘要: ABSTRACT Four substrate analogs—nicotin-amide adenine dinucleotide, adenylyl (3,' 5') guanosine, guanylyl (3',5't) adenosine, and adenoine 2',5’-diphosphate-have been used to prepare the complexes with trichosanthin (TCS), a type I ribosome-inactivating protein that possesses the activity of N-glycosidase. The crystal structures of the coxnpleses have been determined and refined at high resolution. The refined structures show that the N-glyeosidic bonds of’ all the four substrate analogues are hydrolyzed and a common structure is shared by the four complexes, in which only idenine, the product of the enzymatic reaction, is oonnd in the active center. The structure is com-pared with those of native trichosanthin, and a previously reported trichosanthin—NADPH complex in which the N-glycosidic bond is uncleaved. The structural comparison shows that the conformation of Tyr7O obviously differs from those in the latter two structures, I.e., the side chain of Tyrl70 is rotated along its Cβ-Cγ bond by approximately 70? The water molecule found to be preassociated with the N-glycosidic bond in the TCS—NADPH complex struc-ture and proposed to bt the water candidate respon-sible for hydrotyzing the N-glycosidic bond disappears rn the trichosanthin—product complex structure. Based on the comparison of the three structures representing the different stages of the enzymatic reaction, the catalytic mechanism of RNA N-glycosidase has been further elucidated. Proteins
语种: 英语
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WOS记录号: WOS:000085493600004
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/23662
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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Recommended Citation:
Gu YJ,Xia ZX. Crystal structures of the complexes of trichosanthin with four substrate analogs and catalytic mechanism of RNA N-Glycosidase[J]. Proteins: St,2000,Funct., Genet. 2000, 39(1):37-46.
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