6DKF
 
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7KR2
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6VGQ
 | | ClpP1P2 complex from M. tuberculosis with GLF-CMK bound to ClpP1 | | Descriptor: | ATP-dependent Clp protease proteolytic subunit, ATP-dependent Clp protease proteolytic subunit 1, Z-Gly-leu-phe-CH2Cl | | Authors: | Ripstein, Z.A, Vahidi, S, Rubinstein, J.L, Kay, L.E. | | Deposit date: | 2020-01-08 | | Release date: | 2020-03-18 | | Last modified: | 2020-04-01 | | Method: | ELECTRON MICROSCOPY (3.5 Å) | | Cite: | An allosteric switch regulatesMycobacterium tuberculosisClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
Proc.Natl.Acad.Sci.USA, 117, 2020
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6VFX
 | | ClpXP from Neisseria meningitidis - Conformation B | | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ATP-dependent Clp protease ATP-binding subunit ClpX, ... | | Authors: | Ripstein, Z.A, Vahidi, S, Houry, W.A, Rubinstein, J.L, Kay, L.E. | | Deposit date: | 2020-01-06 | | Release date: | 2020-01-22 | | Last modified: | 2024-03-06 | | Method: | ELECTRON MICROSCOPY (2.9 Å) | | Cite: | A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
Elife, 9, 2020
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6VFS
 | | ClpXP from Neisseria meningitidis - Conformation A | | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ATP-dependent Clp protease ATP-binding subunit ClpX, ... | | Authors: | Ripstein, Z.A, Vahidi, S, Houry, W.A, Rubinstein, J.L, Kay, L.E. | | Deposit date: | 2020-01-06 | | Release date: | 2020-01-22 | | Last modified: | 2024-03-06 | | Method: | ELECTRON MICROSCOPY (3.3 Å) | | Cite: | A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
Elife, 9, 2020
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6VGN
 | | ClpP1P2 complex from M. tuberculosis bound to ADEP | | Descriptor: | ATP-dependent Clp protease proteolytic subunit, ATP-dependent Clp protease proteolytic subunit 1, R0M-WFP-ALO-PRO-YCP-ALA-MP8 | | Authors: | Ripstein, Z.A, Vahidi, S, Rubinstein, J.L, Kay, L.E. | | Deposit date: | 2020-01-08 | | Release date: | 2020-03-18 | | Last modified: | 2020-04-01 | | Method: | ELECTRON MICROSCOPY (3.1 Å) | | Cite: | An allosteric switch regulatesMycobacterium tuberculosisClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
Proc.Natl.Acad.Sci.USA, 117, 2020
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6VGK
 | | ClpP1P2 complex from M. tuberculosis | | Descriptor: | ATP-dependent Clp protease proteolytic subunit 1, ATP-dependent Clp protease proteolytic subunit 2 | | Authors: | Ripstein, Z.A, Vahidi, S, Rubinstein, J.L, Kay, L.E. | | Deposit date: | 2020-01-08 | | Release date: | 2020-03-18 | | Last modified: | 2024-03-06 | | Method: | ELECTRON MICROSCOPY (3.1 Å) | | Cite: | An allosteric switch regulatesMycobacterium tuberculosisClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
Proc.Natl.Acad.Sci.USA, 117, 2020
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