2y1q

X-ray diffraction
1.5Å resolution

Crystal Structure of ClpC N-terminal Domain

Released:
Source organism: Bacillus subtilis
Primary publication:
Structure and mechanism of the hexameric MecA-ClpC molecular machine.
Nature 471 331-5 (2011)
PMID: 21368759

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 150 amino acids
Theoretical weight: 16.36 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P37571 (Residues: 1-150; Coverage: 19%)
Gene names: BSU00860, clpC, mecB
Sequence domains: Clp amino terminal domain, pathogenicity island component
Structure domains: Clp, N-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER X8 PROTEUM
Spacegroup: P65
Unit cell:
a: 84.916Å b: 84.916Å c: 31.633Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.17 0.199
Expression system: Escherichia coli