› 6djv

Electron Microscopy
3.9Å resolution

Mtb ClpB in complex with ATPgammaS and casein, Conformer 2

Released:
DOI: 10.2210/pdb6djv/pdb
PDB entry 6djv coloured by chain, front view.
PDB entry 6djv coloured by chain, side view.
PDB entry 6djv coloured by chain, top view.
Source organisms:
Primary publication:
ATP hydrolysis-coupled peptide translocation mechanism of Mycobacterium tuberculosis ClpB.
Yu H, Lupoli TJ, Kovach A, Meng X, Zhao G, Nathan CF, Li H
Proc Natl Acad Sci U S A 115 E9560-E9569 (2018)
PMID: 30257943
Related structures: EMD-7943

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161963 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein ClpB Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 848 amino acids
Theoretical weight: 92.69 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPD1 (Residues: 1-848; Coverage: 100%)
Gene names: MTV036.19c, Rv0384c, clpB
Sequence domains:
casein polyAlanine model Chain: N
Molecule details ›
Chain: N
Length: 26 amino acids
Theoretical weight: 1.87 KDa
Source organism: Bos taurus

Ligands and Environments

2 bound ligands:
Ligand AGS 10 x AGS
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.9Å
Relevant EMDB volumes: EMD-7943
Expression system: Escherichia coli

Quick links

Citations

12 review citations

The molecular principles governing the activity and functional diversity of AAA+ proteins.
Puchades et al. (2020)
11 more

3 mentions without citation

Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation.
Gates et al. (2020)
2 more