2j2z

From Proteopedia

Revision as of 16:18, 5 November 2007

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

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