1efu: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1efu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efu OCA], [http://www.ebi.ac.uk/pdbsum/1efu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1efu RCSB]</span> | |||
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[[Category: elongation factor]] | [[Category: elongation factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:42 2008'' | ||
Revision as of 20:01, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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