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2j2z
From Proteopedia
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|PDB= 2j2z |SIZE=350|CAPTION= <scene name='initialview01'>2j2z</scene>, resolution 2.3Å | |PDB= 2j2z |SIZE=350|CAPTION= <scene name='initialview01'>2j2z</scene>, resolution 2.3Å | ||
|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> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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.]] | ||
| - | [[Category: CO]] | ||
| - | [[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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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| , 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
Page seeded by OCA on Mon Mar 31 03:52:12 2008
