doi: 10.1002/j.1460-2075.1985.tb03943.x.
Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography
- PMID: 3908095
- PMCID: PMC554514
- DOI: 10.1002/j.1460-2075.1985.tb03943.x
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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
EMBO J.
1985 Sep.
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.
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