› 6ed3

Electron Microscopy
6.3Å resolution

Mtb ClpB in complex with AMPPNP

Released:
DOI: 10.2210/pdb6ed3/pdb
PDB entry 6ed3 coloured by chain, front view.
PDB entry 6ed3 coloured by chain, side view.
PDB entry 6ed3 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
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
OpenAccess logo Proc Natl Acad Sci U S A 115 E9560-E9569 (2018)
PMID: 30257943
Related structures: EMD-9028

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161961 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 6.3Å
Relevant EMDB volumes: EMD-9028
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

2 mentions without citation

Recent Insights into the Structure and Function of Mycobacterial Membrane Proteins Facilitated by Cryo-EM.
Bendre et al. (2021)
1 more