› 4h4l

X-ray diffraction
2.5Å resolution

Crystal Structure of ternary complex of HutP(HutP-L-His-Zn)

Released:
DOI: 10.2210/pdb4h4l/pdb
PDB entry 4h4l coloured by chain, front view.
PDB entry 4h4l coloured by chain, side view.
PDB entry 4h4l coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Alternative binding modes of l-histidine guided by metal ions for the activation of the antiterminator protein HutP of Bacillus subtilis.
Dhakshnamoorthy B, Mizuno H, Kumar PKR
J Struct Biol 183 512-518 (2013)
PMID: 23748184

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145533 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hut operon positive regulatory protein Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 148 amino acids
Theoretical weight: 16.23 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P10943 (Residues: 1-148; Coverage: 100%)
Gene names: BSU39340, hutP
Sequence domains: HutP
Structure domains: Hut operon regulatory protein HutP

Ligands and Environments

2 bound ligands:
Ligand HIS 12 x HIS
Ligand ZN 12 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P3
Unit cell:
a: 129.53Å b: 129.53Å c: 76.67Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.219 0.298
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Zinc regulates ERp44-dependent protein quality control in the early secretory pathway.
Watanabe et al. (2019)

1 mention without citation

Metal ion-dependent anti-termination of transcriptional regulation of ribonucleoprotein complexes.
Kumar et al. (2014)