This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1tcs
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1tcs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tcs, resolution 1.7Å" /> '''CRYSTAL STRUCTURE OF ...)
Next diff →
Revision as of 01:02, 21 November 2007
|
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 with NDP as ligand. Active as rRNA N-glycosylase, with EC number 3.2.2.22 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 Wed Nov 21 03:09:37 2007
