2co2
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SALMONELLA ENTERICA SAFA PILIN IN COMPLEX WITH A 19-RESIDUE SAFA NTE PEPTIDE (F3A 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
2CO2 is a Protein complex structure of sequences from Salmonella enterica. 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
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