1EFU

ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI

Summary for 1EFU

Entry DOI	10.2210/pdb1efu/pdb
Descriptor	ELONGATION FACTOR TU, ELONGATION FACTOR TS (3 entities in total)
Functional Keywords	elongation factor, complex (two elongation factors)
Biological source	Escherichia coli More
Total number of polymer chains	4
Total formula weight	145125.93
Authors	Kawashima, T.,Berthet-Colominas, C.,Wulff, M.,Cusack, S.,Leberman, R. (deposition date: 1996-07-09, release date: 1997-01-11, Last modification date: 2024-02-07)
Primary citation	Kawashima, T.,Berthet-Colominas, C.,Wulff, M.,Cusack, S.,Leberman, R. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Nature, 379:511-518, 1996 Cited by PubMed 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. PubMed: 8596629 DOI: 10.1038/379511a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation