Abstract：
: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.
journal_name
Celljournal_title
Cellauthors
Zavialov AV,Berglund J,Pudney AF,Fooks LJ,Ibrahim TM,MacIntyre S,Knight SDdoi
10.1016/s0092-8674(03)00351-9subject
Has Abstractpub_date
2003-05-30 00:00:00pages
587-96issue
5eissn
0092-8674issn
1097-4172pii
S0092867403003519journal_volume
113pub_type
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