1P5U

X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex

Summary for 1P5U

• Entry DOI: 10.2210/pdb1p5u/pdb
• Related: 1P5V
• Descriptor: Chaperone protein Caf1M, F1 capsule antigen, ... (4 entities in total)
• Functional Keywords: chaperone, chaperone-target complex, chaperone-subunit complex, protein fiber, donor strand complementation, donor strand exchange, structural protein
• Biological source: Yersinia pestis; More
• Cellular location: Periplasm: P26926; Secreted, capsule: P26948 P26948
• Total number of polymer chains: 3
• Total formula weight: 57663.51

Authors

Zavialov, A.V.,Berglund, J.,Pudney, A.F.,Fooks, L.J.,Ibrahim, T.M.,MacIntyre, S.,Knight, S.D. (deposition date: 2003-04-28, release date: 2003-06-24, Last modification date: 2024-04-03)

Primary citation

Zavialov, A.V.,Berglund, J.,Pudney, A.F.,Fooks, L.J.,Ibrahim, T.M.,MacIntyre, S.,Knight, S.D.
Structure and Biogenesis of the Capsular F1 Antigen from Yersinia pestis. Preserved Folding Energy Drives Fiber Formation
Cell(Cambridge,Mass.), 113:587-596, 2003

PubMed 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.

PubMed: 12787500
DOI: 10.1016/S0092-8674(03)00351-9

Experimental method

X-RAY DIFFRACTION (1.99 Å)