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6VGQ

ClpP1P2 complex from M. tuberculosis with GLF-CMK bound to ClpP1

Summary for 6VGQ
Entry DOI10.2210/pdb6vgq/pdb
Related6VGK
EMDB information21197 21199
DescriptorATP-dependent Clp protease proteolytic subunit 1, ATP-dependent Clp protease proteolytic subunit, Z-Gly-leu-phe-CH2Cl (3 entities in total)
Functional Keywordscomplex, protease, clpp, tuberculosis, hydrolase
Biological sourceMycobacterium tuberculosis
More
Total number of polymer chains21
Total formula weight304509.38
Authors
Ripstein, Z.A.,Vahidi, S.,Rubinstein, J.L.,Kay, L.E. (deposition date: 2020-01-08, release date: 2020-03-18, Last modification date: 2020-04-01)
Primary citationVahidi, S.,Ripstein, Z.A.,Juravsky, J.B.,Rennella, E.,Goldberg, A.L.,Mittermaier, A.K.,Rubinstein, J.L.,Kay, L.E.
An allosteric switch regulatesMycobacterium tuberculosisClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
Proc.Natl.Acad.Sci.USA, 117:5895-5906, 2020
Cited by
PubMed: 32123115
DOI: 10.1073/pnas.1921630117
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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