› 1yyf

X-ray diffraction
4.16Å resolution

Correction of X-ray Intensities from an HslV-HslU co-crystal containing lattice translocation defects

Released:
DOI: 10.2210/pdb1yyf/pdb
PDB entry 1yyf coloured by chain, front view.
PDB entry 1yyf coloured by chain, side view.
PDB entry 1yyf coloured by chain, top view.
Source organisms:
Primary publication:
Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects.
Wang J, Rho SH, Park HH, Eom SH
Acta Crystallogr D Biol Crystallogr 61 932-41 (2005)
PMID: 15983416

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141350 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent protease ATPase subunit HslU Chains: A, B
Molecule details ›
Chains: A, B
Length: 443 amino acids
Theoretical weight: 49.66 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6H5 (Residues: 1-443; Coverage: 100%)
Gene names: JW3902, b3931, hslU, htpI
Sequence domains:
ATP-dependent protease subunit ClpQ Chains: C, D
Molecule details ›
Chains: C, D
Length: 181 amino acids
Theoretical weight: 19.5 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39070 (Residues: 1-181; Coverage: 100%)
Gene names: BSU16150, clpQ, codW, hslV
Sequence domains: Proteasome subunit

Ligands and Environments

1 bound ligand:
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: R32
Unit cell:
a: 181.196Å b: 181.196Å c: 529.924Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.28 0.277 0.346
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.
Wu et al. (2011)
8 more