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New page: left|200px<br /><applet load="1tig" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tig, resolution 2.0Å" /> '''TRANSLATION INITIATIO...
 
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[[Image:1tig.gif|left|200px]]<br /><applet load="1tig" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1tig.gif|left|200px]]<br /><applet load="1tig" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1tig, resolution 2.0&Aring;" />
caption="1tig, resolution 2.0&Aring;" />
'''TRANSLATION INITIATION FACTOR 3 C-TERMINAL DOMAIN'''<br />
'''TRANSLATION INITIATION FACTOR 3 C-TERMINAL DOMAIN'''<br />


==Overview==
==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.
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==
==About this Structure==
1TIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TIG OCA].  
1TIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIG OCA].  


==Reference==
==Reference==
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[[Category: if3 c-terminal domain]]
[[Category: if3 c-terminal domain]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:49 2008''

Revision as of 13:13, 21 February 2008

File: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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