Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation.
Journal, issue, pages	EMBO J, Vol. 26, Issue 9, Page 2421-2431, Year 2007
Publish date	May 2, 2007
Authors	Derek J Taylor / Jakob Nilsson / A Rod Merrill / Gregers Rom Andersen / Poul Nissen / Joachim Frank /
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 ...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.
External links	EMBO J / PubMed:17446867 / PubMed Central
Methods	EM (single particle)
Resolution	8.9 - 11.7 Å
Structure data	1342 2p8w EMDB-1342: Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation. PDB-2p8w: Fitted structure of eEF2 in the 80S:eEF2:GDPNP cryo-EM reconstruction Method: EM (single particle) / Resolution: 11.3 Å 1343 2p8x EMDB-1343: Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation. PDB-2p8x: Fitted structure of ADPR-eEF2 in the 80S:ADPR-eEF2:GDPNP cryo-EM reconstruction Method: EM (single particle) / Resolution: 9.7 Å 1344 2p8y EMDB-1344: Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation. PDB-2p8y: Fitted structure of ADPR-eEF2 in the 80S:ADPR-eEF2:GDP:sordarin cryo-EM reconstruction Method: EM (single particle) / Resolution: 11.7 Å 1345 2p8z EMDB-1345: Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation. PDB-2p8z: Fitted structure of ADPR-eEF2 in the 80S:ADPR-eEF2:GDPNP:sordarin cryo-EM reconstruction Method: EM (single particle) / Resolution: 8.9 Å
Chemicals	ChemComp-GNP: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogueYM / 5'-Guanylyl imidodiphosphate ChemComp-APR: ADENOSINE-5-DIPHOSPHORIBOSE ChemComp-SO1: [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 ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM / Guanosine diphosphate
Source	saccharomyces cerevisiae (brewer's yeast) Thermomyces lanuginosus (fungus) thermus thermophilus (bacteria)
Keywords	TRANSLATION / elongation / translocation / GTPase / 80S ribosome