1n0l

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[[Image:1n0l.jpg|left|200px]]
[[Image:1n0l.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1n0l |SIZE=350|CAPTION= <scene name='initialview01'>1n0l</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1n0l", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= papD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), papE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1n0l| PDB=1n0l | SCENE= }}
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|RELATEDENTRY=[[1n12|1N12]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n0l OCA], [http://www.ebi.ac.uk/pdbsum/1n0l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n0l RCSB]</span>
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}}
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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'''
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[[Category: Sauer, F G.]]
[[Category: Sauer, F G.]]
[[Category: Waksman, G.]]
[[Category: Waksman, G.]]
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[[Category: chaperone priming]]
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[[Category: Chaperone priming]]
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[[Category: donor strand complemenation]]
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[[Category: Donor strand complemenation]]
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[[Category: donor strand exchange]]
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[[Category: Donor strand exchange]]
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[[Category: immunoglobulin-like fold]]
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[[Category: Immunoglobulin-like fold]]
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[[Category: pilus fiber assembly]]
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[[Category: Pilus fiber assembly]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:56:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:23:39 2008''
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Revision as of 22:56, 2 May 2008

Image:1n0l.jpg

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


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 Page seeded by OCA on Sat May 3 01:56:22 2008

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