3pxi

X-ray diffraction
6.93Å resolution

Structure of MecA108:ClpC

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:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-153435 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Adapter protein MecA 1 Chains: a, b, c
Molecule details ›
Chains: a, b, c
Length: 111 amino acids
Theoretical weight: 13.08 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P37958 (Residues: 108-218; Coverage: 51%)
Gene names: BSU11520, mecA
Sequence domains: Negative regulator of genetic competence (MecA)
Negative regulator of genetic competence ClpC/MecB Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 758 amino acids
Theoretical weight: 84.59 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P37571 (Residues: 1-810; Coverage: 94%)
Gene names: BSU00860, clpC, mecB
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P6522
Unit cell:
a: 141.806Å b: 141.806Å c: 656.078Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.408 0.407 0.422
Expression system: Escherichia coli