1tcs
From Proteopedia
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| , resolution 1.7Å | |||||||
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| Ligands: | |||||||
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF TRICHOSANTHIN-NADPH COMPLEX AT 1.7 ANGSTROMS RESOLUTION REVEALS ACTIVE-SITE ARCHITECTURE
Overview
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.
About this Structure
1TCS is a Single protein structure of sequence from Trichosanthes kirilowii. Full crystallographic information is available from OCA.
Reference
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
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