› 2k77

Solution NMR

NMR solution structure of the Bacillus subtilis ClpC N-domain

Released:
DOI: 10.2210/pdb2k77/pdb
PDB entry 2k77 coloured by chain, ensemble of 30 models, front view.
PDB entry 2k77 coloured by chain, ensemble of 30 models, side view.
PDB entry 2k77 coloured by chain, ensemble of 30 models, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.
Kojetin DJ, McLaughlin PD, Thompson RJ, Dubnau D, Prepiak P, Rance M, Cavanagh J
J Mol Biol 387 639-52 (2009)
PMID: 19361434

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Negative regulator of genetic competence ClpC/MecB Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 15.99 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P37571 (Residues: 1-145; Coverage: 18%)
Gene names: BSU00860, clpC, mecB
Sequence domains: Clp amino terminal domain, pathogenicity island component
Structure domains: Clp, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases.
Kirstein et al. (2009)
3 more

1 mention without citation

Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.
Kojetin et al. (2009)