1ETU

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

Summary for 1ETU

Entry DOI	10.2210/pdb1etu/pdb
Descriptor	ELONGATION FACTOR TU, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywords	transport and protection protein
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	43676.78
Authors	Clark, B.F.C.,Lacour, T.F.M.,Kjeldgaard, M.,Morikawa, K.,Nyborg, J.,Rubin, R.,Thirup, S. (deposition date: 1988-01-15, release date: 1988-07-16, Last modification date: 2024-12-25)
Primary citation	la Cour, T.F.,Nyborg, J.,Thirup, S.,Clark, B.F. Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. EMBO J., 4:2385-2388, 1985 Cited by PubMed 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. PubMed: 3908095 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.9 Å)

Structure validation