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• W2019203602 abstract "PapD is the periplasmic chaperone required for the assembly of P pili in pyelonephritic strains of Escherichia coli. It consists of two immunoglobulin-like domains bisected by a subunit binding cleft. PapD is the prototype member of a super family of immunoglobulin-like chaperones that work in concert with their respective ushers to assemble a plethora of adhesive organelles including pilus- and non-pilus-associated adhesins. Three highly conserved residue clusters have been shown to play critical roles in the structure and function of PapD, as determined by site-directed mutagenesis. The in vivo stability of the chaperone depended on the formation of a buried salt bridge within the cleft. Residues along the G1 beta strand were required for efficient binding of subunits consistent with the crystal structure of PapD-peptide complexes. Finally, Thr-53, a residue that is part of a conserved band of residues located on the amino-terminal domain surface opposite the subunit binding cleft, was also found to be critical for pilus assembly, but mutations at Thr-53 did not interfere with chaperone-subunit complex formation." @default.
• W2019203602 created "2016-06-24" @default.
• W2019203602 creator A5007679233 @default.
• W2019203602 creator A5035728249 @default.
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• W2019203602 date "1999-02-01" @default.
• W2019203602 modified "2023-10-15" @default.
• W2019203602 title "Probing conserved surfaces on PapD" @default.
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• W2019203602 doi "https://doi.org/10.1046/j.1365-2958.1999.01216.x" @default.
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