1etu

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File:1etu.gif


1etu, resolution 2.9Å

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STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE DIPHOSPHATE TO ELONGATION FACTOR TU FROM E. COLI AS STUDIED BY X-RAY CRYSTALLOGRAPHY

OverviewOverview

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.

About this StructureAbout this Structure

1ETU is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography., la Cour TF, Nyborg J, Thirup S, Clark BF, EMBO J. 1985 Sep;4(9):2385-8. PMID:3908095

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