This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2c77
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="2c77" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c77, resolution 1.60Å" /> '''EF-TU COMPLEXED WIT...)
Next diff →
Revision as of 14:37, 29 October 2007
|
EF-TU COMPLEXED WITH A GTP ANALOG AND THE ANTIBIOTIC GE2270 A
Overview
Pulvomycin inhibits protein synthesis by preventing the formation of the, ternary complex between elongation factor Tu (EF-Tu) x GTP and aa-tRNA. In, this work, the crystal structure of Thermus thermophilus EF-Tu x, pulvomycin in complex with the GTP analogue guanylyl imino diphosphate, (GDPNP) at 1.4 A resolution reveals an antibiotic binding site extending, from the domain 1-3 interface to domain 2, overlapping the domain 1-2-3, junction. Pulvomycin binding interferes with the binding of the, 3'-aminoacyl group, the acceptor stem, and 5' end of tRNA. Only part of, pulvomycin overlaps the binding site of GE2270 A, a domain 2-bound, antibiotic of a structure unrelated to pulvomycin, which also hinders, aa-tRNA binding. The structure of the T. thermophilus EF-Tu x GDPNP x, GE2270 A complex ... [(full description)]
About this Structure
2C77 is a [Single protein] structure of sequence from [Thermus thermophilus] with MG, GNP, GEA and PEG as [ligands]. Active as [[1]], with EC number [3.1.5.1]. Full crystallographic information is available from [OCA].
Reference
Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu., Parmeggiani A, Krab IM, Okamura S, Nielsen RC, Nyborg J, Nissen P, Biochemistry. 2006 Jun 6;45(22):6846-57. PMID:16734421
Page seeded by OCA on Mon Oct 29 16:42:24 2007
Categories: Single protein | Thermus thermophilus | Krab, I.M. | Nielsen, R.C. | Nissen, P. | Nyborg, J. | Okamura, S. | Parmeggiani, A. | GEA | GNP | MG | PEG | Antibiotic | Gtp-binding | Gtpase | Hydrolase | Nucleotide-binding | Phosphorylation | Protein biosynthesis | Protein synthesis | Translation elongation factor
