1n0l
From Proteopedia
(New page: 200px<br /><applet load="1n0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n0l, resolution 2.30Å" /> '''Crystal structure of...) |
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| - | [[Image:1n0l.jpg|left|200px]]<br /><applet load="1n0l" size=" | + | [[Image:1n0l.jpg|left|200px]]<br /><applet load="1n0l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n0l, resolution 2.30Å" /> | caption="1n0l, resolution 2.30Å" /> | ||
'''Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli'''<br /> | '''Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Periplasmic chaperones direct the assembly of adhesive, multi-subunit | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1N0L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1N0L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Hultgren, S | + | [[Category: Hultgren, S J.]] |
| - | [[Category: Pinkner, J | + | [[Category: Pinkner, J S.]] |
| - | [[Category: Sauer, F | + | [[Category: Sauer, F G.]] |
[[Category: Waksman, G.]] | [[Category: Waksman, G.]] | ||
[[Category: chaperone priming]] | [[Category: chaperone priming]] | ||
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[[Category: pilus fiber assembly]] | [[Category: pilus fiber assembly]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:59 2008'' |
Revision as of 12:01, 21 February 2008
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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
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.
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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