2j2z
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 2J2Z is a | + | 2J2Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and CO as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J2Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pilus termination]] | [[Category: pilus termination]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:32:48 2007'' |
Revision as of 10:27, 5 November 2007
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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 with SO4 and CO as ligands. Structure known Active Site: AC1. 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 Nov 5 12:32:48 2007
