Resolving the energy paradox of chaperone/usher-mediated fibre assembly.

ABSTRACT: Periplasmic chaperone/usher machineries are used for assembly of filamentous adhesion organelles of Gram-negative pathogens in a process that has been suggested to be driven by folding energy. Structures of mutant chaperone-subunit complexes revealed a final folding transition (condensation of the subunit hydrophobic core) on the release of organelle subunit from the chaperone-subunit pre-assembly complex and incorporation into the final fibre structure. However, in view of the large interface between chaperone and subunit in the pre-assembly complex and the reported stability of this complex, it is difficult to understand how final folding could release sufficient energy to drive assembly. In the present paper, we show the X-ray structure for a native chaperone-fibre complex that, togethe

SUBMITTER: Zavialov AV 

PROVIDER: S-EPMC1180718 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature