1k3s: Difference between revisions

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[[Image:1k3s.~~jpg~~|left|200px]]

[[Image:1k3s.png|left|200px]]

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~~'''~~Type III Secretion Chaperone SigE~~'''~~

===Type III Secretion Chaperone SigE===

~~==Overview==~~

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~~Several Gram-negative bacterial pathogens have evolved a type III secretion system~~ to deliver virulence effector proteins directly into eukaryotic cells, a process essential for disease. This specialized secretion process requires customized chaperones specific for particular effector proteins. The crystal structures of the ~~enterohemorrhagic Escherichia coli O157~~:~~H7 Tir-specific chaperone CesT and the Salmonella enterica SigD-specific chaperone SigE reveal a common overall fold and formation of homodimers~~. ~~Site-directed mutagenesis suggests that variable~~, ~~delocalized hydrophobic surfaces observed on~~ the ~~chaperone homodimers are responsible for specific binding to a particular effector protein~~. ~~Isothermal titration calorimetry studies of Tir~~-~~CesT and enzymatic activity profiles of SigD~~-~~SigE indicate that the effector proteins are not globally unfolded in the presence of their cognate chaperones.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11685226}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11685226 is the PubMed ID number.

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==About this Structure==

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[[Category: Sige]]

[[Category: Type iii]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 22:16:10 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 03:43:02 2008''

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-[[Image:1k3s.jpg|left|200px]]
+{{Seed}}
+[[Image:1k3s.png|left|200px]]
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 {{STRUCTURE_1k3s|  PDB=1k3s  |  SCENE=  }}
-'''Type III Secretion Chaperone SigE'''
+===Type III Secretion Chaperone SigE===
-==Overview==
+<!--
-Several Gram-negative bacterial pathogens have evolved a type III secretion system to deliver virulence effector proteins directly into eukaryotic cells, a process essential for disease. This specialized secretion process requires customized chaperones specific for particular effector proteins. The crystal structures of the enterohemorrhagic Escherichia coli O157:H7 Tir-specific chaperone CesT and the Salmonella enterica SigD-specific chaperone SigE reveal a common overall fold and formation of homodimers. Site-directed mutagenesis suggests that variable, delocalized hydrophobic surfaces observed on the chaperone homodimers are responsible for specific binding to a particular effector protein. Isothermal titration calorimetry studies of Tir-CesT and enzymatic activity profiles of SigD-SigE indicate that the effector proteins are not globally unfolded in the presence of their cognate chaperones.
+The line below this paragraph, {{ABSTRACT_PUBMED_11685226}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11685226 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11685226}}
 ==About this Structure==
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 [[Category: Sige]]
 [[Category: Type iii]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:16:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 03:43:02 2008''