3zgx

X-ray diffraction
3.4Å resolution

Crystal structure of the kleisin-N SMC interface in prokaryotic condensin

Released:
Source organism: Bacillus subtilis
Primary publication:
An asymmetric SMC-kleisin bridge in prokaryotic condensin.
Nat Struct Mol Biol 20 371-9 (2013)
PMID: 23353789

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-152806 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chromosome partition protein Smc Chains: A, B
Molecule details ›
Chains: A, B
Length: 426 amino acids
Theoretical weight: 48.17 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P51834 (Residues: 1-219, 223-1186; Coverage: 36%)
Gene names: BSU15940, smc, ylqA
Sequence domains: RecF/RecN/SMC N terminal domain
Structure domains:
Segregation and condensation protein A Chains: C, Z
Molecule details ›
Chains: C, Z
Length: 94 amino acids
Theoretical weight: 11.18 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P35154 (Residues: 1-86; Coverage: 34%)
Gene names: BSU23220, scpA, ypuG
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P43
Unit cell:
a: 107.435Å b: 107.435Å c: 102.821Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.243 0.277
Expression system: Escherichia coli BL21