Structural highlights
Function
[RIPT_TRIKI] Inactivates eukaryotic 60S ribosomal subunits.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We describe here the crystal structure of the trichosanthin-NADPH complex determined at a resolution of 1.7 A. 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.
Crystal structure of trichosanthin-NADPH complex at 1.7 A resolution reveals active-site architecture.,Xiong JP, Xia ZX, Wang Y Nat Struct Biol. 1994 Oct;1(10):695-700. PMID:7634073[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xiong JP, Xia ZX, Wang Y. Crystal structure of trichosanthin-NADPH complex at 1.7 A resolution reveals active-site architecture. Nat Struct Biol. 1994 Oct;1(10):695-700. PMID:7634073
