1tig

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Image:1tig.gif

1tig, resolution 2.0Å

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TRANSLATION INITIATION FACTOR 3 C-TERMINAL DOMAIN

Overview

The structures of the two domains of translational initiation factor IF3, from Bacillus stearothermophilus have been solved by X-ray crystallography, using single wavelength anomalous scattering and multiwavelength anomalous, diffraction. Each of the two domains has an alpha/beta topology, with an, exposed beta-sheet that is reminiscent of several ribosomal and other RNA, binding proteins. An alpha-helix that protrudes out from the body of the, N-terminal domain towards the C-terminal domain suggests that IF3 consists, of two RNA binding domains connected by an alpha-helix and that it may, bridge two regions of the ribosome. This represents the first high, resolution structural information on a translational initiation factor.

About this Structure

1TIG is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix., Biou V, Shu F, Ramakrishnan V, EMBO J. 1995 Aug 15;14(16):4056-64. PMID:7664745

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