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6VFS

ClpXP from Neisseria meningitidis - Conformation A

Summary for 6VFS
Entry DOI10.2210/pdb6vfs/pdb
Related6VFX
EMDB information21187 21194
DescriptorATP-dependent Clp protease ATP-binding subunit ClpX, Unidentified protein substrate, ATP-dependent Clp protease proteolytic subunit, ... (6 entities in total)
Functional Keywordscomplex, aaa+, protease, clpp, clpx, hydrolase
Biological sourceNeisseria meningitidis
More
Total number of polymer chains21
Total formula weight592650.26
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 citationRipstein, 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
Cited by
PubMed: 31916936
DOI: 10.7554/eLife.52158
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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