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6VGN

ClpP1P2 complex from M. tuberculosis bound to ADEP

Summary for 6VGN
Entry DOI10.2210/pdb6vgn/pdb
Related6VGK
EMDB information21197 21198
DescriptorATP-dependent Clp protease proteolytic subunit, ATP-dependent Clp protease proteolytic subunit 1, R0M-WFP-ALO-PRO-YCP-ALA-MP8 (3 entities in total)
Functional Keywordscomplex, protease, clpp, tuberculosis, hydrolase, hydrolase-antibiotic complex, hydrolase/antibiotic
Biological sourceMycobacterium tuberculosis
More
Total number of polymer chains21
Total formula weight306472.45
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 (3.1 Å)
Structure validation

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