1u2r
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(New page: 200px<br /><applet load="1u2r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u2r, resolution 2.6Å" /> '''Crystal Structure of ...)
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Revision as of 01:41, 21 November 2007
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Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae
Overview
The crystal structure of ADP-ribosylated yeast elongation factor 2 in the, presence of sordarin and GDP has been determined at 2.6 A resolution. The, diphthamide at the tip of domain IV, which is the target for diphtheria, toxin and Pseudomonas aeruginosa exotoxin A, contains a covalently, attached ADP-ribose that functions as a very potent inhibitor of the, factor. We have obtained an electron density map of ADP-ribosylated, translation factor 2 revealing both the ADP-ribosylation and the, diphthamide. This is the first structure showing the conformation of an, ADP-ribosylated residue and confirms the inversion of configuration at the, glycosidic linkage. Binding experiments show that the ADP-ribosylation has, limited effect on nucleotide binding affinity, on ribosome binding, and on, association with exotoxin A. These results provide insight to the, inhibitory mechanism and suggest that inhibition may be caused by, erroneous interaction of the translation factor with the codon-anticodon, area in the P-site of the ribosome.
About this Structure
1U2R is a Single protein structure of sequence from Saccharomyces cerevisiae with MG, APR, SO1 and GDP as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of ADP-ribosylated ribosomal translocase from Saccharomyces cerevisiae., Jorgensen R, Yates SP, Teal DJ, Nilsson J, Prentice GA, Merrill AR, Andersen GR, J Biol Chem. 2004 Oct 29;279(44):45919-25. Epub 2004 Aug 16. PMID:15316019
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