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Crystal structure of trichosanthin-NADPH complex at 1.7Å resolution reveals active-site architecture

Nature Structural Biology volume 1, pages 695–700 (1994)Cite this article

Abstract

We describe here the crystal structure of the trichosanthin-NADPH complex determined at a resolution of 1.7 Å. The adenine base stacks between Tyr 70 and Tyr 111. Arg 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 N-glycosidic bond is well defined and the preassociated water, thought to be responsible for hydrolyzing the N-C bond, is also explicitly elucidated.

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  1. Jian-Ping Xiong

    Present address: Howard Hughes Medical Institute Research Laboratories Institute of Molecular Biology, University of Oregon Eugene, Oregon, 97403, USA

Authors and Affiliations

  1. Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 200032, China

    Zong-Xiang Xia & Yu Wang

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  1. Jian-Ping Xiong
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  2. Zong-Xiang Xia
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Xiong, JP., Xia, ZX. & Wang, Y. Crystal structure of trichosanthin-NADPH complex at 1.7Å resolution reveals active-site architecture. Nat Struct Mol Biol 1, 695–700 (1994). https://doi.org/10.1038/nsb1094-695

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