6vfs | pdb_00006vfs
ClpXP from Neisseria meningitidis - Conformation A
Structural highlights
Function[A0A0Y4ZJG4_NEIME] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175][SAAS:SAAS01076750] [A0A0Y5K536_NEIME] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.[HAMAP-Rule:MF_00444][RuleBase:RU000550][SAAS:SAAS00674840] Publication Abstract from PubMedThe 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 Neisseria meningitidis at 2.3 to 3.3 A 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. A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.,Ripstein ZA, Vahidi S, Houry WA, Rubinstein JL, Kay LE Elife. 2020 Jan 9;9. pii: 52158. doi: 10.7554/eLife.52158. PMID:31916936[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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