1ob5

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1ob5, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

T. AQUATICUS ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC ENACYLOXIN IIA, A GTP ANALOG, AND PHE-TRNA

Overview

Elongation factor (EF-) Tu.GTP is the carrier of aminoacyl-tRNA to the, programmed ribosome. Enacyloxin IIa inhibits bacterial protein synthesis, by hindering the release of EF-Tu.GDP from the ribosome. The crystal, structure of the Escherichia coli EF-Tu.guanylyl iminodiphosphate, (GDPNP).enacyloxin IIa complex at 2.3 A resolution presented here reveals, the location of the antibiotic at the interface of domains 1 and 3. The, binding site overlaps that of kirromycin, an antibiotic with a structure, that is unrelated to enacyloxin IIa but that also inhibits EF-Tu.GDP, release. As one of the major differences, the enacyloxin IIa tail borders, a hydrophobic pocket that is occupied by the longer tail of kirromycin, explaining the higher binding affinity of the latter., EF-Tu.GDPNP.enacyloxin ... [(full description)]

About this Structure

1OB5 is a [Protein complex] structure of sequences from [Thermus aquaticus] with MG, C, PHA, GNP and ENX as [ligands]. Active as [Transferred entry: 3.6.5.3], with EC number [3.6.1.48]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibiotics., Parmeggiani A, Krab IM, Watanabe T, Nielsen RC, Dahlberg C, Nyborg J, Nissen P, J Biol Chem. 2006 Feb 3;281(5):2893-900. Epub 2005 Oct 28. PMID:16257965

Page seeded by OCA on Tue Oct 30 15:48:39 2007