2nsb: Difference between revisions

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[[Image:2nsb.~~gif~~|left|200px]]

[[Image:2nsb.png|left|200px]]

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~~'''~~Structures of and interactions between domains of trigger factor from Themotoga maritima~~'''~~

===Structures of and interactions between domains of trigger factor from Themotoga maritima===

~~==Overview==~~

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~~Trigger factor (TF) is a eubacterial chaperone that associates with ribosomes at the peptide~~-~~exit tunnel and also occurs in excess free in the cytosol. TF is a three~~-domain protein that appears to exist in a dynamic equilibrium of oligomerization states and interdomain conformations. X-ray crystallography and chemical cross-linking were used to study the roles of the N- and C-terminal domains of Thermotoga maritima TF in TF oligomerization and chaperone activity. The ~~structural conservation of both~~ the ~~N- and C-terminal TF domains was unambiguously established. The biochemical and crystallographic data reveal a tendency for these domains~~ to ~~partake in diverse and apparently nonspecific protein-protein interactions. It is found that~~ the T. ~~maritima and Escherichia coli TF surfaces lack evident exposed hydrophobic patches~~. ~~Taken together~~, ~~these data suggest that TF chaperones could interact with nascent proteins via hydrophilic surfaces~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17372359}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17372359 is the PubMed ID number.

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==About this Structure==

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[[Category: Martinez-Hackert, E.]]

[[Category: Chaperone]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu May~~ 22 ~~22:26~~:11 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:22:40 2008''

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-[[Image:2nsb.gif|left|200px]]
+{{Seed}}
+[[Image:2nsb.png|left|200px]]
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 {{STRUCTURE_2nsb|  PDB=2nsb  |  SCENE=  }}
-'''Structures of and interactions between domains of trigger factor from Themotoga maritima'''
+===Structures of and interactions between domains of trigger factor from Themotoga maritima===
-==Overview==
+<!--
-Trigger factor (TF) is a eubacterial chaperone that associates with ribosomes at the peptide-exit tunnel and also occurs in excess free in the cytosol. TF is a three-domain protein that appears to exist in a dynamic equilibrium of oligomerization states and interdomain conformations. X-ray crystallography and chemical cross-linking were used to study the roles of the N- and C-terminal domains of Thermotoga maritima TF in TF oligomerization and chaperone activity. The structural conservation of both the N- and C-terminal TF domains was unambiguously established. The biochemical and crystallographic data reveal a tendency for these domains to partake in diverse and apparently nonspecific protein-protein interactions. It is found that the T. maritima and Escherichia coli TF surfaces lack evident exposed hydrophobic patches. Taken together, these data suggest that TF chaperones could interact with nascent proteins via hydrophilic surfaces.
+The line below this paragraph, {{ABSTRACT_PUBMED_17372359}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17372359 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17372359}}
 ==About this Structure==
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 [[Category: Martinez-Hackert, E.]]
 [[Category: Chaperone]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:26:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:22:40 2008''