2j2z

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[[Image:2j2z.gif|left|200px]]<br />
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[[Image:2j2z.jpg|left|200px]]<br /><applet load="2j2z" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="2j2z" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2j2z, resolution 2.3&Aring;" />
caption="2j2z, resolution 2.3&Aring;" />
'''X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION'''<br />
'''X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION'''<br />
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==About this Structure==
==About this Structure==
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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].
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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]. Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain B'>AC1</scene>. 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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 18:23:49 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:46:09 2007''

Revision as of 17:36, 18 December 2007


2j2z, resolution 2.3Å

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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. Known structural/functional Site: . 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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