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1efu
From Proteopedia
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| - | [[Image:1efu.jpg|left|200px]] | + | [[Image:1efu.jpg|left|200px]] |
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| - | '''ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1efu |SIZE=350|CAPTION= <scene name='initialview01'>1efu</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EFU is a [ | + | 1EFU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1EFU with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFU OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8596629 8596629] |
[[Category: Elongation Factors]] | [[Category: Elongation Factors]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: elongation factor]] | [[Category: elongation factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:55:01 2008'' |
Revision as of 08:55, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI
Overview
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 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.
Reference
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 Thu Mar 20 10:55:01 2008
