6VGQ
ClpP1P2 complex from M. tuberculosis with GLF-CMK bound to ClpP1
Summary for 6VGQ
Entry DOI | 10.2210/pdb6vgq/pdb |
Related | 6VGK |
EMDB information | 21197 21199 |
Descriptor | ATP-dependent Clp protease proteolytic subunit 1, ATP-dependent Clp protease proteolytic subunit, Z-Gly-leu-phe-CH2Cl (3 entities in total) |
Functional Keywords | complex, protease, clpp, tuberculosis, hydrolase |
Biological source | Mycobacterium tuberculosis More |
Total number of polymer chains | 21 |
Total formula weight | 304509.38 |
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 citation | Vahidi, 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: 32123115DOI: 10.1073/pnas.1921630117 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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