Zavialov, Anton
- Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
Sammanfattning
Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation
Publicerad i
Cell
2003, volym: 113, nummer: 5, sidor: 587-596
Utgivare: CELL PRESS
SLU författare
Berglund, Jenny
- Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
- Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
Knight, Stefan David
- Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
- Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
UKÄ forskningsämne
Livsmedelsvetenskap
Publikationens identifierare
- DOI: https://doi.org/10.1016/S0092-8674(03)00351-9
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/141