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2j2z
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(New page: 200px<br /> <applet load="2j2z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j2z, resolution 2.3Å" /> '''X-RAY STRUCTURE OF T...)
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Revision as of 14:05, 29 October 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 ... [(full description)]
About this Structure
2J2Z is a [Protein complex] structure of sequences from [Escherichia coli] with SO4 and CO as [ligands]. 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 Oct 29 16:10:29 2007
