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PMID: 3908095 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography.

The EMBO journal ·Vol. 4 ·No. 9 ·1985-09-00 ·Pages 2385-8

la Cour TF, Nyborg J, Thirup S, Clark BF

Abstract

Structural details of the guanosine diphosphate binding to a modified form of elongation factor Tu from Escherichia coli, resulting from X-ray crystallographic studies, are reported. The protein elements that take part in the nucleotide binding are located in four loops connecting beta-strands with alpha-helices. These loops correspond to regions in primary sequences which show a high degree of homology when compared with other prokaryotic and eukaryotic elongation factors and initiation factor 2.

MeSH Terms
Escherichia coli/genetics,metabolism Guanine Nucleotides/metabolism Guanosine Diphosphate/metabolism Models, Molecular Nucleic Acid Conformation Peptide Elongation Factor Tu/metabolism Protein Binding Protein Conformation X-Ray Diffraction
Chemicals
Guanine Nucleotides Guanosine Diphosphate Peptide Elongation Factor Tu
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
la Cour T F
Nyborg J
Thirup S
Clark B F
References (31)
31 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1985-09-00
Pages
2385-8
Language
English
Region
England
NLM ID
8208664
PMCID
PMC554514
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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