1efu: Difference between revisions
New page: left|200px<br /> <applet load="1efu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1efu, resolution 2.5Å" /> '''ELONGATION FACTOR CO... |
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[[Image:1efu. | [[Image:1efu.jpg|left|200px]]<br /><applet load="1efu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1efu, resolution 2.5Å" /> | caption="1efu, resolution 2.5Å" /> | ||
'''ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI'''<br /> | '''ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1EFU is a [http://en.wikipedia.org/wiki/Protein_complex 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:// | 1EFU is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: elongation factor]] | [[Category: elongation factor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:43:01 2008'' | ||
Revision as of 16:43, 15 February 2008
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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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