View source for 1efu

[[Image:1efu.jpg|left|200px]]<br /><applet load="1efu" size="350" color="white" frame="true" align="right" spinBox="true" 
caption="1efu, resolution 2.5&Aring;" />
'''ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI'''<br />

==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 [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==
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8596629 8596629]
[[Category: Elongation Factors]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Berthet-Colominas, C.]]
[[Category: Cusack, S.]]
[[Category: Kawashima, T.]]
[[Category: Leberman, R.]]
[[Category: Wulff, M.]]
[[Category: complex (two elongation factors)]]
[[Category: elongation factor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:43:01 2008''