{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Remaut H"],"funding":["Medical Research Council","Biotechnology and Biological Sciences Research Council"],"pagination":["831-842"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7617774"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(6)"],"pubmed_abstract":["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 "],"journal":["Molecular cell"],"pubmed_title":["Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism."],"pmcid":["PMC7617774"],"funding_grant_id":["SF16972","G0100442"],"pubmed_authors":["Radford SE","Rose RJ","Waksman G","Hultgren SJ","Remaut H","Hannan TJ","Ashcroft AE"],"additional_accession":[]},"is_claimable":false,"name":"Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism.","description":"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 ","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Jun","modification":"2026-06-03T07:56:38.649Z","creation":"2026-04-26T03:10:45.846Z"},"accession":"S-EPMC7617774","cross_references":{"pubmed":["16793551"],"doi":["10.1016/j.molcel.2006.05.033"]}}