6VFS

ClpXP from Neisseria meningitidis - Conformation A

Summary for 6VFS

• Entry DOI: 10.2210/pdb6vfs/pdb
• Related: 6VFX
• EMDB information: 21187 21194
• Descriptor: ATP-dependent Clp protease ATP-binding subunit ClpX, Unidentified protein substrate, ATP-dependent Clp protease proteolytic subunit, ... (6 entities in total)
• Functional Keywords: complex, aaa+, protease, clpp, clpx, hydrolase
• Biological source: Neisseria meningitidis; More
• Total number of polymer chains: 21
• Total formula weight: 592650.26

Authors

Ripstein, Z.A.,Vahidi, S.,Houry, W.A.,Rubinstein, J.L.,Kay, L.E. (deposition date: 2020-01-06, release date: 2020-01-22, Last modification date: 2024-03-06)

Primary citation

Ripstein, Z.A.,Vahidi, S.,Houry, W.A.,Rubinstein, J.L.,Kay, L.E.
A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
Elife, 9:-, 2020

PubMed Abstract: The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins. ClpXP is an important target for drug development against infectious diseases. Although structures are available for isolated ClpX and ClpP rings, it remains unknown how symmetry mismatched ClpX and ClpP work in tandem for processive substrate translocation into the ClpP proteolytic chamber. Here, we present cryo-EM structures of the substrate-bound ClpXP complex from at 2.3 to 3.3 Å resolution. The structures allow development of a model in which the sequential hydrolysis of ATP is coupled to motions of ClpX loops that lead to directional substrate translocation and ClpX rotation relative to ClpP. Our data add to the growing body of evidence that AAA+ molecular machines generate translocating forces by a common mechanism.

PubMed: 31916936
DOI: 10.7554/eLife.52158

Experimental method

ELECTRON MICROSCOPY (3.3 Å)