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PMID: 19833920 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA.

Science (New York, N.Y.) ·Vol. 326 ·No. 5953 ·2009-10-30 ·Pages 688-694

Schmeing TM, Voorhees RM, Kelley AC, Gao YG, Murphy FV, Weir JR, Ramakrishnan V

Abstract

The ribosome selects a correct transfer RNA (tRNA) for each amino acid added to the polypeptide chain, as directed by messenger RNA. Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. The signaling pathway that leads to GTP hydrolysis upon codon recognition is critical to accurate decoding. Here we present the crystal structure of the ribosome complexed with EF-Tu and aminoacyl-tRNA, refined to 3.6 angstrom resolution. The structure reveals details of the tRNA distortion that allows aminoacyl-tRNA to interact simultaneously with the decoding center of the 30S subunit and EF-Tu at the factor binding site. A series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathway between the decoding center and the guanosine triphosphatase center of EF-Tu.

MeSH Terms
Crystallography, X-Ray Enzyme Activation GTP Phosphohydrolases/metabolism Genetic Code Models, Molecular Nucleic Acid Conformation Peptide Elongation Factor Tu/chemistry Protein Binding Protein Conformation Protein Structure, Tertiary RNA, Bacterial/chemistry RNA, Transfer, Amino Acyl/chemistry RNA, Transfer, Phe/chemistry RNA, Transfer, Thr/chemistry Ribosomes/chemistry Thermus thermophilus
Chemicals
RNA, Bacterial RNA, Transfer, Amino Acyl RNA, Transfer, Phe RNA, Transfer, Thr GTP Phosphohydrolases Peptide Elongation Factor Tu
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Schmeing T Martin
MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Voorhees Rebecca M
MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Kelley Ann C
MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Gao Yong-Gui
MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Murphy Frank V
MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Weir John R
MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
Ramakrishnan V
MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
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Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
1095-9203
DOI
10.1126/science.1179700
Published
2009-10-30
Epub
2009-00-15
Pages
688-694
Language
English
Region
United States
NLM ID
0404511
PMCID
PMC3763470
Subset
IM
Grants
Wellcome Trust · 082086 · United Kingdom
Medical Research Council · MC_U105184332 · United Kingdom
Databases
PDB
2WRN, 2WRO, 2WRQ, 2WRR
Corrections
CommentIn
PMID: 19833922
External Links
PubMed source DOI: 10.1126/science.1179700 PMC Full Text View journal details
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