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2j2z

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[[Image:2j2z.jpg|left|200px]]
[[Image:2j2z.jpg|left|200px]]
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{{Structure
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|PDB= 2j2z |SIZE=350|CAPTION= <scene name='initialview01'>2j2z</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_2j2z", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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{{STRUCTURE_2j2z| PDB=2j2z | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j2z OCA], [http://www.ebi.ac.uk/pdbsum/2j2z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j2z RCSB]</span>
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'''X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION'''
'''X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION'''
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[[Category: Verger, D.]]
[[Category: Verger, D.]]
[[Category: Waksman, G.]]
[[Category: Waksman, G.]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: chaperone/ surface active protein complex]]
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[[Category: Chaperone/ surface active protein complex]]
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[[Category: fimbria]]
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[[Category: Fimbria]]
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[[Category: immunoglobulin domain]]
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[[Category: Immunoglobulin domain]]
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[[Category: p5 pocket]]
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[[Category: P5 pocket]]
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[[Category: papd]]
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[[Category: Papd]]
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[[Category: paph]]
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[[Category: Paph]]
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[[Category: periplasmic]]
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[[Category: Periplasmic]]
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[[Category: pilus termination]]
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[[Category: Pilus termination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:15:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:12 2008''
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Revision as of 05:15, 4 May 2008

Template:STRUCTURE 2j2z

X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION


Overview

P pili are important adhesive fibres that are assembled by the conserved chaperone-usher pathway. During pilus assembly, the subunits are incorporated into the growing fibre by the donor-strand exchange mechanism, whereby the beta-strand of the chaperone, which complements the incomplete immunoglobulin fold of each subunit, is displaced by the amino-terminal extension of an incoming subunit in a zip-in-zip-out exchange process that is initiated at the P5 pocket, an exposed hydrophobic pocket in the groove of the subunit. In vivo, termination of P pilus growth requires a specialized subunit, PapH. Here, we show that PapH is incorporated at the base of the growing pilus, where it is unable to undergo donor-strand exchange. This inability is not due to a stronger PapD-PapH interaction, but to a lack of a P5 initiator pocket in the PapH structure, suggesting that PapH terminates pilus growth because it is lacking the initiation point by which donor-strand exchange proceeds.

About this Structure

2J2Z is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Molecular mechanism of P pilus termination in uropathogenic Escherichia coli., Verger D, Miller E, Remaut H, Waksman G, Hultgren S, EMBO Rep. 2006 Dec;7(12):1228-32. Epub 2006 Nov 3. PMID:17082819 Page seeded by OCA on Sun May 4 08:15:43 2008

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