1n0l: Difference between revisions

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[[Image:1n0l.jpg|left|200px]]
{{Seed}}
[[Image:1n0l.png|left|200px]]


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{{STRUCTURE_1n0l|  PDB=1n0l  |  SCENE=  }}  
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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.
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{{ABSTRACT_PUBMED_12437927}}


==About this Structure==
==About this Structure==
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[[Category: Immunoglobulin-like fold]]
[[Category: Immunoglobulin-like fold]]
[[Category: Pilus fiber assembly]]
[[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''

Revision as of 02:34, 29 July 2008

File:1n0l.png

Template:STRUCTURE 1n0l

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

Template:ABSTRACT PUBMED 12437927

About this Structure

1N0L is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation., Sauer FG, Pinkner JS, Waksman G, Hultgren SJ, Cell. 2002 Nov 15;111(4):543-51. PMID:12437927

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