2y1r

X-ray diffraction
2.6Å resolution

Structure of MecA121 & ClpC N-domain complex

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-153434 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Negative regulator of genetic competence ClpC/MecB Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 149 amino acids
Theoretical weight: 16.23 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P37571 (Residues: 1-149; Coverage: 18%)
Gene names: BSU00860, clpC, mecB
Sequence domains: Clp amino terminal domain, pathogenicity island component
Structure domains: Clp, N-terminal domain
Adapter protein MecA 1 Chains: I, J, K, L, M, N, O, P
Molecule details ›
Chains: I, J, K, L, M, N, O, P
Length: 98 amino acids
Theoretical weight: 11.53 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P37958 (Residues: 121-218; Coverage: 45%)
Gene names: BSU11520, mecA
Sequence domains: Negative regulator of genetic competence (MecA)
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 110.02Å b: 124.72Å c: 149.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.213 0.258
Expression system: Escherichia coli