1ory: Difference between revisions

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[[Image:1ory.~~gif~~|left|200px]]

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

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~~'''~~FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER~~'''~~

===FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER===

~~==Overview==~~

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~~Assembly of~~ the ~~bacterial flagellum and type III secretion in pathogenic bacteria require cytosolic export chaperones that interact with mobile components~~ to ~~facilitate their secretion. Although their amino acid sequences are not conserved,~~ the structures of several type III secretion chaperones revealed striking similarities between their folds and modes of substrate recognition. Here, we report the first crystallographic structure of a flagellar export chaperone, Aquifex aeolicus FliS. ~~FliS adopts a novel fold that is clearly distinct from those of the type III secretion chaperones, indicating that they do not share a common evolutionary origin~~. ~~However, the structure of FliS in complex with a fragment of FliC (flagellin~~) ~~reveals that~~, ~~like~~ the ~~type III secretion chaperones, flagellar export chaperones bind their target proteins in extended conformation and suggests that this mode of recognition may be widely used in bacteria~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12958592}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12958592 is the PubMed ID number.

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==About this Structure==

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[[Category: Flic]]

[[Category: Fli]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 04~~:12:34 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:01:21 2008''

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-[[Image:1ory.gif|left|200px]]
+{{Seed}}
+[[Image:1ory.png|left|200px]]
 <!--
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 {{STRUCTURE_1ory|  PDB=1ory  |  SCENE=  }}
-'''FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER'''
+===FLAGELLAR EXPORT CHAPERONE IN COMPLEX WITH ITS COGNATE BINDING PARTNER===
-==Overview==
+<!--
-Assembly of the bacterial flagellum and type III secretion in pathogenic bacteria require cytosolic export chaperones that interact with mobile components to facilitate their secretion. Although their amino acid sequences are not conserved, the structures of several type III secretion chaperones revealed striking similarities between their folds and modes of substrate recognition. Here, we report the first crystallographic structure of a flagellar export chaperone, Aquifex aeolicus FliS. FliS adopts a novel fold that is clearly distinct from those of the type III secretion chaperones, indicating that they do not share a common evolutionary origin. However, the structure of FliS in complex with a fragment of FliC (flagellin) reveals that, like the type III secretion chaperones, flagellar export chaperones bind their target proteins in extended conformation and suggests that this mode of recognition may be widely used in bacteria.
+The line below this paragraph, {{ABSTRACT_PUBMED_12958592}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12958592 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12958592}}
 ==About this Structure==
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 [[Category: Flic]]
 [[Category: Fli]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:12:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:01:21 2008''