2j2z

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|PDB= 2j2z |SIZE=350|CAPTION= <scene name='initialview01'>2j2z</scene>, resolution 2.3&Aring;
|PDB= 2j2z |SIZE=350|CAPTION= <scene name='initialview01'>2j2z</scene>, resolution 2.3&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CO:COBALT (II) ION'>CO</scene>
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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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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[[Category: Verger, D.]]
[[Category: Verger, D.]]
[[Category: Waksman, G.]]
[[Category: Waksman, G.]]
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[[Category: CO]]
 
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[[Category: SO4]]
 
[[Category: chaperone]]
[[Category: chaperone]]
[[Category: chaperone/ surface active protein complex]]
[[Category: chaperone/ surface active protein complex]]
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[[Category: pilus termination]]
[[Category: pilus termination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:36:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:12 2008''

Revision as of 00:52, 31 March 2008


PDB ID 2j2z

Drag the structure with the mouse to rotate
, resolution 2.3Å
Sites:
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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