1t11
From Proteopedia
(New page: 200px<br /><applet load="1t11" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t11, resolution 2.50Å" /> '''Trigger Factor'''<br...) |
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| - | [[Image:1t11.gif|left|200px]]<br /><applet load="1t11" size=" | + | [[Image:1t11.gif|left|200px]]<br /><applet load="1t11" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t11, resolution 2.50Å" /> | caption="1t11, resolution 2.50Å" /> | ||
'''Trigger Factor'''<br /> | '''Trigger Factor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Trigger factor is a molecular chaperone that is present in all species of | + | Trigger factor is a molecular chaperone that is present in all species of eubacteria. It binds to the ribosomal 50S subunit near the translation exit tunnel and is thought to be the first protein to interact with nascent polypeptides emerging from the ribosome. The chaperone has a peptidyl-prolyl cis-trans isomerase (PPIase) activity that catalyzes the rate-limiting proline isomerization in the protein-folding process. We have determined the crystal structure of nearly full-length trigger factor from Vibrio cholerae by x-ray crystallography at 2.5-A resolution. The structure is composed of two trigger-factor molecules related by a noncrystallographic two-fold symmetry axis. The monomer has an elongated shape and is folded into three domains: an N-terminal domain I that binds to the ribosome, a central domain II that contains PPIase activity, and a C-terminal domain III. The active site of the PPIase domain is occupied by a loop from domain III, suggesting that the PPIase activity of the protein could be regulated. The dimer interface is formed between domains I and III and contains residues of mixed properties. Further implications about dimerization, ribosome binding, and other functions of trigger factor are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1T11 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http:// | + | 1T11 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T11 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
| - | [[Category: Ludlam, A | + | [[Category: Ludlam, A V.]] |
| - | [[Category: Moore, B | + | [[Category: Moore, B A.]] |
[[Category: Xu, Z.]] | [[Category: Xu, Z.]] | ||
[[Category: four-helix-bundle]] | [[Category: four-helix-bundle]] | ||
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[[Category: ppiase]] | [[Category: ppiase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:43 2008'' |
Revision as of 13:08, 21 February 2008
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Trigger Factor
Overview
Trigger factor is a molecular chaperone that is present in all species of eubacteria. It binds to the ribosomal 50S subunit near the translation exit tunnel and is thought to be the first protein to interact with nascent polypeptides emerging from the ribosome. The chaperone has a peptidyl-prolyl cis-trans isomerase (PPIase) activity that catalyzes the rate-limiting proline isomerization in the protein-folding process. We have determined the crystal structure of nearly full-length trigger factor from Vibrio cholerae by x-ray crystallography at 2.5-A resolution. The structure is composed of two trigger-factor molecules related by a noncrystallographic two-fold symmetry axis. The monomer has an elongated shape and is folded into three domains: an N-terminal domain I that binds to the ribosome, a central domain II that contains PPIase activity, and a C-terminal domain III. The active site of the PPIase domain is occupied by a loop from domain III, suggesting that the PPIase activity of the protein could be regulated. The dimer interface is formed between domains I and III and contains residues of mixed properties. Further implications about dimerization, ribosome binding, and other functions of trigger factor are discussed.
About this Structure
1T11 is a Single protein structure of sequence from Vibrio cholerae. Full crystallographic information is available from OCA.
Reference
The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae., Ludlam AV, Moore BA, Xu Z, Proc Natl Acad Sci U S A. 2004 Sep 14;101(37):13436-41. Epub 2004 Sep 7. PMID:15353602
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