Chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii

Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information.

Residues 4 to 12 in the mature protein (29 to 37 in the full sequence before signal peptide removal)
were replaced by a 6H-coding fragment to produce a N-terminal hexa-histag.

Chaperone of the Csu biofilm-mediating pili of Acinetobacter baumannii

Major pilus subunit from the Csu biofilm-mediating pili of Acinetobacter baumannii

Backbone resonance assignment (HN, N, Ca, Cb and CO) of CsuC-CsuA/B chaperone-major subunit
pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii.

Backbone resonance assignments for the CsuC-CsuA/B complex.

Crystal structure of CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii

500 M [U- 2H, 13C, 15N] CsuC-CsuA/B in 50 mM sodium phosphate pH 6.0, 50 mM NaCl, 10% D2O.

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax