2co3: Difference between revisions

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[[Image:2co3.gif|left|200px]]
[[Image:2co3.gif|left|200px]]


{{Structure
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{{STRUCTURE_2co3| PDB=2co3  | SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2co3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2co3 OCA], [http://www.ebi.ac.uk/pdbsum/2co3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2co3 RCSB]</span>
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'''SALMONELLA ENTERICA SAFA PILIN, HEAD-TO-TAIL SWAPPED DIMER OF NTD1 MUTANT'''
'''SALMONELLA ENTERICA SAFA PILIN, HEAD-TO-TAIL SWAPPED DIMER OF NTD1 MUTANT'''
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[[Category: Rose, R J.]]
[[Category: Rose, R J.]]
[[Category: Waksman, G.]]
[[Category: Waksman, G.]]
[[Category: adhesion]]
[[Category: Adhesion]]
[[Category: fibril protein]]
[[Category: Fibril protein]]
[[Category: fold complementation]]
[[Category: Fold complementation]]
[[Category: pathogenesis]]
[[Category: Pathogenesis]]
[[Category: pilus subunit]]
[[Category: Pilus subunit]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:38:27 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:24:15 2008''

Revision as of 22:38, 3 May 2008

File:2co3.gif

Template:STRUCTURE 2co3

SALMONELLA ENTERICA SAFA PILIN, HEAD-TO-TAIL SWAPPED DIMER OF NTD1 MUTANT


OverviewOverview

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.

About this StructureAbout this Structure

2CO3 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

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 Sat May 3 22:38:27 2008

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