1n0l: Difference between revisions

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[[Image:1n0l.png|left|200px]]

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~~'''~~Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli~~'''~~

===Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli===

~~==Overview==~~

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~~Periplasmic chaperones direct the assembly of adhesive~~, ~~multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which~~ the ~~N-terminal extension of one subunit replaces~~ the ~~chaperone G~~(~~1) strand that transiently occupies a groove in the neighboring subunit~~. ~~Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation~~. ~~During donor strand exchange~~, ~~the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It~~ is ~~this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into~~ the ~~fiber~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12437927}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12437927 is the PubMed ID number.

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==About this Structure==

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[[Category: Immunoglobulin-like fold]]

[[Category: Pilus fiber assembly]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 01~~:56:22 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:34:16 2008''

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-[[Image:1n0l.jpg|left|200px]]
+{{Seed}}
+[[Image:1n0l.png|left|200px]]
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 {{STRUCTURE_1n0l|  PDB=1n0l  |  SCENE=  }}
-'''Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli'''
+===Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli===
-==Overview==
+<!--
-Periplasmic chaperones direct the assembly of adhesive, multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which the N-terminal extension of one subunit replaces the chaperone G(1) strand that transiently occupies a groove in the neighboring subunit. Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It is this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into the fiber.
+The line below this paragraph, {{ABSTRACT_PUBMED_12437927}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12437927 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12437927}}
 ==About this Structure==
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 [[Category: Immunoglobulin-like fold]]
 [[Category: Pilus fiber assembly]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:56:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:34:16 2008''