2P8Y
Fitted structure of ADPR-eEF2 in the 80S:ADPR-eEF2:GDP:sordarin cryo-EM reconstruction
Summary for 2P8Y
Entry DOI | 10.2210/pdb2p8y/pdb |
Related | 1K5X 1K5Y 2P8w 2P8x 2P8z |
EMDB information | 1344 |
Descriptor | Elongation factor 2, ADENOSINE-5-DIPHOSPHORIBOSE, [1R-(1.ALPHA.,3A.BETA.,4.BETA.,4A.BETA.,7.BETA.,7A.ALPHA.,8A.BETA.)]8A-[(6-DEOXY-4-O-METHYL-BETA-D-ALTROPYRANOSYLOXY)METHYL]-4-FORMYL-4,4A,5,6,7,7A,8,8A-OCTAHYDRO-7-METHYL-3-(1-METHYLETHYL)-1,4-METHANO-S-INDACENE-3A(1H)-CARBOXYLIC ACID, ... (4 entities in total) |
Functional Keywords | elongation, translocation, gtpase, 80s ribosome, translation |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Total number of polymer chains | 1 |
Total formula weight | 95046.46 |
Authors | Taylor, D.J.,Nilsson, J.,Merrill, A.R.,Andersen, G.R.,Nissen, P.,Frank, J. (deposition date: 2007-03-23, release date: 2007-05-08, Last modification date: 2019-12-18) |
Primary citation | Taylor, D.J.,Nilsson, J.,Merrill, A.R.,Andersen, G.R.,Nissen, P.,Frank, J. Structures of modified eEF2.80S ribosome complexes reveal the role of GTP hydrolysis in translocation. Embo J., 26:2421-2431, 2007 Cited by PubMed Abstract: On the basis of kinetic data on ribosome protein synthesis, the mechanical energy for translocation of the mRNA-tRNA complex is thought to be provided by GTP hydrolysis of an elongation factor (eEF2 in eukaryotes, EF-G in bacteria). We have obtained cryo-EM reconstructions of eukaryotic ribosomes complexed with ADP-ribosylated eEF2 (ADPR-eEF2), before and after GTP hydrolysis, providing a structural basis for analyzing the GTPase-coupled mechanism of translocation. Using the ADP-ribosyl group as a distinct marker, we observe conformational changes of ADPR-eEF2 that are due strictly to GTP hydrolysis. These movements are likely representative of native eEF2 motions in a physiological context and are sufficient to uncouple the mRNA-tRNA complex from two universally conserved bases in the ribosomal decoding center (A1492 and A1493 in Escherichia coli) during translocation. Interpretation of these data provides a detailed two-step model of translocation that begins with the eEF2/EF-G binding-induced ratcheting motion of the small ribosomal subunit. GTP hydrolysis then uncouples the mRNA-tRNA complex from the decoding center so translocation of the mRNA-tRNA moiety may be completed by a head rotation of the small subunit. PubMed: 17446867DOI: 10.1038/sj.emboj.7601677 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (11.7 Å) |
Structure validation
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