2c77
From Proteopedia
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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 [dGTPase], with EC number [3.1.5.1]. Structure known Active Site: AC1. 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 Tue Oct 30 10:43:20 2007
Categories: Single protein | Thermus thermophilus | DGTPase | 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
