› 3qph

X-ray diffraction
2.99Å resolution

The three-dimensional structure of TrmB, a global transcriptional regulator of the hyperthermophilic archaeon Pyrococcus furiosus in complex with sucrose

Released:
DOI: 10.2210/pdb3qph/pdb
PDB entry 3qph coloured by chain, front view.
PDB entry 3qph coloured by chain, side view.
PDB entry 3qph coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
The three-dimensional structure of TrmB, a transcriptional regulator of dual function in the hyperthermophilic archaeon Pyrococcus furiosus in complex with sucrose.
Krug M, Lee SJ, Boos W, Diederichs K, Welte W
Protein Sci 22 800-8 (2013)
PMID: 23576322

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
HTH-type sugar sensing transcriptional regulator TrmB Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 39.34 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HGZ9 (Residues: 1-338; Coverage: 100%)
Gene names: PF1743, trmB
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
2 bound ligands:
Ligand ACT 2 x ACT
Ligand GOL 9 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3221
Unit cell:
a: 158.522Å b: 158.522Å c: 79.153Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.226 0.261
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The TrmB family: a versatile group of transcriptional regulators in Archaea.
Gindner et al. (2014)
3 more

4 mentions without citation

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
3 more