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1zm2

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[[Image:1zm2.gif|left|200px]]<br /><applet load="1zm2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zm2.gif|left|200px]]
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caption="1zm2, resolution 3.07&Aring;" />
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'''Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA'''<br />
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{{Structure
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|PDB= 1zm2 |SIZE=350|CAPTION= <scene name='initialview01'>1zm2</scene>, resolution 3.07&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>
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|ACTIVITY=
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|GENE= eta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
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}}
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'''Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZM2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=APR:'>APR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZM2 OCA].
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1ZM2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZM2 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16107839 16107839]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16107839 16107839]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:37:10 2008''

Revision as of 13:37, 20 March 2008


PDB ID 1zm2

Drag the structure with the mouse to rotate
, resolution 3.07Å
Ligands:
Gene: eta (Pseudomonas aeruginosa)
Coordinates: save as pdb, mmCIF, xml



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

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