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[[Image:1zm2.gif|left|200px]]
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{{STRUCTURE_1zm2|  PDB=1zm2  |  SCENE=  }}
'''Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA'''


==Structure of ADP-ribosylated eEF2 in complex with catalytic fragment of ETA==
<StructureSection load='1zm2' size='340' side='right'caption='[[1zm2]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zm2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] and [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZM2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.07&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=DDE:{3-[4-(2-AMINO-2-CARBOXY-ETHYL)-1H-IMIDAZOL-2-YL]-1-CARBAMOYL-PROPYL}-TRIMETHYL-AMMONIUM'>DDE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zm2 OCA], [https://pdbe.org/1zm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zm2 RCSB], [https://www.ebi.ac.uk/pdbsum/1zm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zm2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EF2_YEAST EF2_YEAST]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zm/1zm2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zm2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:16107839</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1zm2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
[[Category: Protein complex]]
*[[Exotoxin 3D structures|Exotoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Andersen, G R.]]
[[Category: Andersen GR]]
[[Category: Boesen, T.]]
[[Category: Boesen T]]
[[Category: Joergensen, R.]]
[[Category: Joergensen R]]
[[Category: Marquez, V E.]]
[[Category: Marquez VE]]
[[Category: Merrill, A R.]]
[[Category: Merrill AR]]
[[Category: Schwan, A L.]]
[[Category: Schwan AL]]
[[Category: Yates, S P.]]
[[Category: Yates SP]]
[[Category: Adp-ribosylation]]
[[Category: Elongation factor]]
[[Category: Toxin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:47:35 2008''
Retrieved from "https://proteopedia.org/1zm2"