1efu: Difference between revisions

Revision as of 15:02, 2 May 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1EFU is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 1EFU with [Elongation Factors]. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 15:02:45 2008

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OCA

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 [[Image:1efu.jpg|left|200px]]
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 [[Category: Leberman, R.]]
 [[Category: Wulff, M.]]
-[[Category: complex (two elongation factors)]]
+[[Category: Elongation factor]]
-[[Category: elongation factor]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:02:45 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:42 2008''