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PMID: 8596629 Published · ppublish English Journal Article

The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.

Nature ·Vol. 379 ·No. 6565 ·1996-02-08 ·Pages 511-8

Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R

Abstract

The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dimer, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.

MeSH Terms
Amino Acid Sequence Crystallography, X-Ray Escherichia coli/chemistry Guanosine Diphosphate/chemistry Magnesium/chemistry Models, Molecular Molecular Sequence Data Peptide Elongation Factor Tu/chemistry Peptide Elongation Factors/chemistry Protein Binding Protein Conformation Protein Structure, Secondary
Chemicals
Peptide Elongation Factors elongation factor Ts Guanosine Diphosphate Peptide Elongation Factor Tu Magnesium
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kawashima T
European Molecular Biology Laboratory, Grenoble Outstation, France.
Berthet-Colominas C
Wulff M
Cusack S
Leberman R
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1996-02-08
Pages
511-8
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
ErratumIn
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CommentIn
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