1zm2

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{{STRUCTURE_1zm2| PDB=1zm2 | SCENE= }}
{{STRUCTURE_1zm2| PDB=1zm2 | SCENE= }}
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'''Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA'''
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===Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16107839}}
==About this Structure==
==About this Structure==
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[[Category: Elongation factor]]
[[Category: Elongation factor]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:47:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:51:27 2008''

Revision as of 08:51, 28 July 2008

Template:STRUCTURE 1zm2

Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA

Template:ABSTRACT PUBMED 16107839

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

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