1zm3: Difference between revisions

Revision as of 07:22, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zm3.png

Template:STRUCTURE 1zm3

Structure of the apo eEF2-ETA complexStructure of the apo eEF2-ETA complex

Template:ABSTRACT PUBMED 16107839

About this StructureAbout this Structure

1ZM3 is a Protein complex structure of sequences from Pseudomonas aeruginosa and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Exotoxin A-eEF2 complex structure indicates ADP ribosylation by ribosome mimicry., Jorgensen R, Merrill AR, Yates SP, Marquez VE, Schwan AL, Boesen T, Andersen GR, Nature. 2005 Aug 18;436(7053):979-84. PMID:16107839

Page seeded by OCA on Tue Jul 29 07:22:26 2008

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OCA

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-'''Structure of the apo eEF2-ETA complex'''
+===Structure of the apo eEF2-ETA complex===
-==Overview==
+<!--
-The bacteria causing diphtheria, whooping cough, cholera and other diseases secrete mono-ADP-ribosylating toxins that modify intracellular proteins. Here, we describe four structures of a catalytically active complex between a fragment of Pseudomonas aeruginosa exotoxin A (ETA) and its protein substrate, translation elongation factor 2 (eEF2). The target residue in eEF2, diphthamide (a modified histidine), spans across a cleft and faces the two phosphates and a ribose of the non-hydrolysable NAD+ analogue, betaTAD. This suggests that the diphthamide is involved in triggering NAD+ cleavage and interacting with the proposed oxacarbenium intermediate during the nucleophilic substitution reaction, explaining the requirement of diphthamide for ADP ribosylation. Diphtheria toxin may recognize eEF2 in a manner similar to ETA. Notably, the toxin-bound betaTAD phosphates mimic the phosphate backbone of two nucleotides in a conformational switch of 18S rRNA, thereby achieving universal recognition of eEF2 by ETA.
+The line below this paragraph, {{ABSTRACT_PUBMED_16107839}}, adds the Publication Abstract to the page
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 [[Category: Elongation factor]]
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