1d1n
From Proteopedia
(New page: 200px<br /><applet load="1d1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d1n" /> '''SOLUTION STRUCTURE OF THE FMET-TRNAFMET BIND...) |
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| - | [[Image:1d1n.gif|left|200px]]<br /><applet load="1d1n" size=" | + | [[Image:1d1n.gif|left|200px]]<br /><applet load="1d1n" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1d1n" /> | caption="1d1n" /> | ||
'''SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2'''<br /> | '''SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of | + | The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel beta-strands, connected via loops, and forms a closed beta-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu small middle dotaminoacyl-tRNA small middle dot GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2. |
==About this Structure== | ==About this Structure== | ||
| - | 1D1N 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:// | + | 1D1N 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=1D1N OCA]. |
==Reference== | ==Reference== | ||
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[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:02 2008'' |
Revision as of 10:12, 21 February 2008
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SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2
Overview
The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel beta-strands, connected via loops, and forms a closed beta-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu small middle dotaminoacyl-tRNA small middle dot GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.
About this Structure
1D1N is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2., Meunier S, Spurio R, Czisch M, Wechselberger R, Guenneugues M, Gualerzi CO, Boelens R, EMBO J. 2000 Apr 17;19(8):1918-26. PMID:10775275
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