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PMID: 8805530 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

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

Structure (London, England : 1993) ·Vol. 4 ·No. 3 ·1996-03-15 ·Pages 229-38

Abel K, Jurnak F

Abstract

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.

MeSH Terms

Guanosine Diphosphate/metabolism,physiology Models, Molecular Molecular Mimicry Molecular Structure Peptide Chain Elongation, Translational/physiology Peptide Elongation Factor Tu/chemistry Peptide Elongation Factors/chemistry Protein Conformation RNA, Transfer, Phe/metabolism Ribosomes/physiology

Chemicals

Peptide Elongation Factors RNA, Transfer, Phe elongation factor Ts Guanosine Diphosphate Peptide Elongation Factor Tu

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Abel K

Department of Biochemistry, University of California, Riverside, CA 92507, USA.

Jurnak F

Article Info

Journal

Structure (London, England : 1993)

Abbr.

Structure

ISSN

0969-2126

DOI

10.1016/S0969-2126(96)00027-5

Published

1996-03-15

Pages

229-38

Language

English

Region

United States

NLM ID

101087697

Subset

Grants

NIGMS NIH HHS · GM26895 · United States

External Links

PubMed source DOI: 10.1016/S0969-2126(96)00027-5 View journal details

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

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