Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release.

ABSTRACT: The highly conserved, 300-kDa cylindrical protease ClpP is an important component of the cellular protein quality machinery. It consists of 14 subunits arranged into two heptameric rings that enclose a large chamber containing the protease active sites. ClpP associates with ClpX and ClpA ATPases that unfold and translocate substrates into the protease catalytic chamber through axial pores located at both ends of the ClpP cylinder. Although the pathway of substrate delivery is well established, the pathway of product release is unknown. Here, we use recently developed transverse relaxation optimized spectroscopy (TROSY) of methyl groups to show that the interface between the heptameric rings exchanges between two structurally distinct conformations. The conformational exchange process has b

SUBMITTER: Sprangers R 

PROVIDER: S-EPMC1283831 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature