1tcs
From Proteopedia
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'''CRYSTAL STRUCTURE OF TRICHOSANTHIN-NADPH COMPLEX AT 1.7 ANGSTROMS RESOLUTION REVEALS ACTIVE-SITE ARCHITECTURE''' | '''CRYSTAL STRUCTURE OF TRICHOSANTHIN-NADPH COMPLEX AT 1.7 ANGSTROMS RESOLUTION REVEALS ACTIVE-SITE ARCHITECTURE''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trichosanthes kirilowii]] | [[Category: Trichosanthes kirilowii]] | ||
- | [[Category: | + | [[Category: RRNA N-glycosylase]] |
[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
[[Category: Xia, Z X.]] | [[Category: Xia, Z X.]] | ||
[[Category: Xiong, J P.]] | [[Category: Xiong, J P.]] | ||
- | [[Category: | + | [[Category: Toxin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:48:06 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 06:48, 3 May 2008
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 Page seeded by OCA on Sat May 3 09:48:06 2008