Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2P8Y

Fitted structure of ADPR-eEF2 in the 80S:ADPR-eEF2:GDP:sordarin cryo-EM reconstruction

Summary for 2P8Y
Entry DOI10.2210/pdb2p8y/pdb
Related1K5X 1K5Y 2P8w 2P8x 2P8z
EMDB information1344
DescriptorElongation 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 Keywordselongation, translocation, gtpase, 80s ribosome, translation
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Total number of polymer chains1
Total formula weight95046.46
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 citationTaylor, 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: 17446867
DOI: 10.1038/sj.emboj.7601677
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (11.7 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon