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1tig
From Proteopedia
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[[Image:1tig.gif|left|200px]] | [[Image:1tig.gif|left|200px]] | ||
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'''TRANSLATION INITIATION FACTOR 3 C-TERMINAL DOMAIN''' | '''TRANSLATION INITIATION FACTOR 3 C-TERMINAL DOMAIN''' | ||
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[[Category: Ramakrishnan, V.]] | [[Category: Ramakrishnan, V.]] | ||
[[Category: Shu, F.]] | [[Category: Shu, F.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:59:08 2008'' | |
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Revision as of 06:59, 3 May 2008
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 Page seeded by OCA on Sat May 3 09:59:08 2008
