1efu | pdb_00001efu
From Proteopedia
ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.,Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R Nature. 1996 Feb 8;379(6565):511-8. PMID:8596629[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 20:13, 22 December 2014.