A complex profile of protein elongation: translating chemical energy into molecular movement

The recently solved structures of the protein elongation factor complexes, EF-Tu–GDPNP–phenylalanyl-tRNA and EF-T–Ts, complete the atomic profile of four EF-Tu conformational states. As a set, the three-dimensional structures suggest an atomic model for movement during protein elongation and, by mol...

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Bibliographic Details
Published inStructure Vol. 4; no. 3; pp. 229 - 238
Main Authors Abel, Kenton, Jurnak, Frances
Format Book Review Journal Article
LanguageEnglish
Published United States Elsevier Inc 15.03.1996
Subjects
Guanosine Diphosphate - metabolism
Guanosine Diphosphate - physiology
Models, Molecular
Molecular Mimicry
Molecular Structure
Peptide Chain Elongation, Translational - physiology
Peptide Elongation Factor Tu - chemistry
Peptide Elongation Factors - chemistry
Protein Conformation
Ribosomes - physiology
RNA, Transfer, Phe - metabolism
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Summary:The recently solved structures of the protein elongation factor complexes, EF-Tu–GDPNP–phenylalanyl-tRNA and EF-T–Ts, complete the atomic profile of four EF-Tu conformational states. As a set, the three-dimensional structures suggest an atomic model for movement during protein elongation and, by molecular mimicry with EF-G, translocation as well.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:0969-2126
1878-4186
DOI:10.1016/S0969-2126(96)00027-5