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2co4

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[[Image:2co4.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2co4| PDB=2co4 | SCENE= }}
{{STRUCTURE_2co4| PDB=2co4 | SCENE= }}
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'''SALMONELLA ENTERICA SAFA PILIN IN COMPLEX WITH A 19-RESIDUE SAFA NTE PEPTIDE'''
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===SALMONELLA ENTERICA SAFA PILIN IN COMPLEX WITH A 19-RESIDUE SAFA NTE PEPTIDE===
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==Overview==
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Gram-negative pathogens commonly use the chaperone-usher pathway to assemble adhesive multisubunit fibers on their surface. In the periplasm, subunits are stabilized by a chaperone that donates a beta strand to complement the subunits' truncated immunoglobulin-like fold. Pilus assembly proceeds through a "donor-strand exchange" (DSE) mechanism whereby this complementary beta strand is replaced by the N-terminal extension (Nte) of an incoming pilus subunit. Using X-ray crystallography and real-time electrospray ionization mass spectrometry (ESI-MS), we demonstrate that DSE requires the formation of a transient ternary complex between the chaperone-subunit complex and the Nte of the next subunit to be assembled. The process is crucially dependent on an initiation site (the P5 pocket) needed to recruit the incoming Nte. The data also suggest a capping reaction displacing DSE toward product formation. These results support a zip-in-zip-out mechanism for DSE and a catalytic role for the usher, the molecular platform at which pili are assembled.
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The line below this paragraph, {{ABSTRACT_PUBMED_16793551}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16793551 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16793551}}
==About this Structure==
==About this Structure==
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[[Category: Fold complementation]]
[[Category: Fold complementation]]
[[Category: Pilus subunit adhesion pathogenesis]]
[[Category: Pilus subunit adhesion pathogenesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:38:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:48:02 2008''

Revision as of 21:48, 28 July 2008

Image:2co4.png

Template:STRUCTURE 2co4

SALMONELLA ENTERICA SAFA PILIN IN COMPLEX WITH A 19-RESIDUE SAFA NTE PEPTIDE

Template:ABSTRACT PUBMED 16793551

About this Structure

2CO4 is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism., Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G, Mol Cell. 2006 Jun 23;22(6):831-42. PMID:16793551

Page seeded by OCA on Tue Jul 29 00:48:02 2008

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