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1ha3

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[[Category: ribosome]]
[[Category: ribosome]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:40:08 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:33:25 2007''

Revision as of 13:28, 30 October 2007

Image:1ha3.gif

1ha3, resolution 2.00Å

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ELONGATION FACTOR TU IN COMPLEX WITH AURODOX

Overview

Aurodox is a member of the family of kirromycin antibiotics, which inhibit, protein biosynthesis by binding to elongation factor Tu (EF-Tu). We have, determined the crystal structure of the 1:1:1 complex of Thermus, thermophilus EF-Tu with GDP and aurodox to 2.0-A resolution. During its, catalytic cycle, EF-Tu adopts two strikingly different conformations, depending on the nucleotide bound: the GDP form and the GTP form. In the, present structure, a GTP complex-like conformation of EF-Tu is observed, although GDP is bound to the nucleotide-binding site. This is consistent, with previous proposals that aurodox fixes EF-Tu on the ribosome by, locking it in its GTP form. Binding of EF-Tu.GDP to aminoacyl-tRNA and, mutually exclusive binding of kirromycin and elongation factor Ts to EF-Tu, ... [(full description)]

About this Structure

1HA3 is a [Single protein] structure of sequence from [Thermus aquaticus] with MG, GDP, MAU and BME as [ligands]. Active as [dGTPase], with EC number [3.1.5.1]. Structure known Active Sites: GDA, GDB, MAA, MAB, MGA and MGB. Full crystallographic information is available from [OCA].

Reference

Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox., Vogeley L, Palm GJ, Mesters JR, Hilgenfeld R, J Biol Chem. 2001 May 18;276(20):17149-55. Epub 2001 Jan 30. PMID:11278992

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