2vqi: Difference between revisions

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[[Image:2vqi.~~jpg~~|left|200px]]

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

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~~'''~~STRUCTURE OF THE P PILUS USHER (PAPC) TRANSLOCATION PORE~~'''~~

===STRUCTURE OF THE P PILUS USHER (PAPC) TRANSLOCATION PORE===

~~==Overview==~~

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~~Gram-negative pathogens commonly exhibit adhesive pili on their surfaces that mediate specific attachment~~ to the ~~host~~. ~~A major class of pili is assembled via the chaperone/usher pathway~~. ~~Here~~, ~~the structural basis for pilus fiber assembly and secretion performed by the outer membrane assembly platform--the usher--~~is ~~revealed by~~ the crystal structure of the translocation domain of the P pilus usher PapC and single particle cryo-electron microscopy imaging of the FimD usher bound to a translocating type 1 pilus assembly intermediate. ~~These structures provide molecular snapshots of a twinned~~-~~pore translocation machinery in action. Unexpectedly, only one pore is used for secretion, while both usher protomers are used for chaperone~~-subunit complex recruitment. The translocating pore itself comprises 24 beta strands and is occluded by a folded plug domain, likely gated by a conformationally constrained beta-hairpin. These structures capture the secretion of a virulence factor across the outer membrane of gram-negative bacteria.

The line below this paragraph, {{ABSTRACT_PUBMED_18485872}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18485872 is the PubMed ID number.

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==About this Structure==

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[[Category: Transport]]

[[Category: Usher]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed May~~ 28 09:16:41 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:20:53 2008''

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-[[Image:2vqi.jpg|left|200px]]
+{{Seed}}
+[[Image:2vqi.png|left|200px]]
 <!--
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 {{STRUCTURE_2vqi|  PDB=2vqi  |  SCENE=  }}
-'''STRUCTURE OF THE P PILUS USHER (PAPC) TRANSLOCATION PORE'''
+===STRUCTURE OF THE P PILUS USHER (PAPC) TRANSLOCATION PORE===
-==Overview==
+<!--
-Gram-negative pathogens commonly exhibit adhesive pili on their surfaces that mediate specific attachment to the host. A major class of pili is assembled via the chaperone/usher pathway. Here, the structural basis for pilus fiber assembly and secretion performed by the outer membrane assembly platform--the usher--is revealed by the crystal structure of the translocation domain of the P pilus usher PapC and single particle cryo-electron microscopy imaging of the FimD usher bound to a translocating type 1 pilus assembly intermediate. These structures provide molecular snapshots of a twinned-pore translocation machinery in action. Unexpectedly, only one pore is used for secretion, while both usher protomers are used for chaperone-subunit complex recruitment. The translocating pore itself comprises 24 beta strands and is occluded by a folded plug domain, likely gated by a conformationally constrained beta-hairpin. These structures capture the secretion of a virulence factor across the outer membrane of gram-negative bacteria.
+The line below this paragraph, {{ABSTRACT_PUBMED_18485872}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18485872 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18485872}}
 ==About this Structure==
@@ Line 40: / Line 44: @@
 [[Category: Transport]]
 [[Category: Usher]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:16:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:20:53 2008''