1zm2
From Proteopedia
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[[Image:1zm2.gif|left|200px]] | [[Image:1zm2.gif|left|200px]] | ||
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'''Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA''' | '''Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA''' | ||
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[[Category: Schwan, A L.]] | [[Category: Schwan, A L.]] | ||
[[Category: Yates, S P.]] | [[Category: Yates, S P.]] | ||
- | [[Category: | + | [[Category: Adp-ribosylation]] |
- | [[Category: | + | [[Category: Elongation factor]] |
- | [[Category: | + | [[Category: Toxin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:47:35 2008'' | |
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Revision as of 14:47, 3 May 2008
Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA
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.
About this Structure
1ZM2 is a Protein complex structure of sequences from Pseudomonas aeruginosa and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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 Sat May 3 17:47:35 2008