› 2fk5

X-ray diffraction
1.9Å resolution

Crystal structure of l-fuculose-1-phosphate aldolase from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb2fk5/pdb
PDB entry 2fk5 coloured by chain, front view.
PDB entry 2fk5 coloured by chain, side view.
PDB entry 2fk5 coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8.
Jeyakanthan J, Taka J, Kikuchi A, Kuroishi C, Yutani K, Shiro Y
Acta Crystallogr Sect F Struct Biol Cryst Commun 61 1075-7 (2005)
PMID: 16511238

Function and Biology Details

Reaction catalysed: 
L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo octamer
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177856 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Class II aldolase/adducin N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 21.62 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SHB9 (Residues: 1-200; Coverage: 100%)
Gene name: TTHA1811
Sequence domains: Class II Aldolase and Adducin N-terminal domain
Structure domains: Class II aldolase/adducin N-terminal domain

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P4
Unit cell:
a: 100.944Å b: 100.944Å c: 45.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.233
Expression system: Escherichia coli

Quick links

Citations

1 review citation

DHAP-dependent aldolases from (hyper)thermophiles: biochemistry and applications.
Falcicchio et al. (2014)
2 other articles

3 mentions without citation

Analysis of protein thermostability enhancing factors in industrially important thermus bacteria species.
Kumwenda et al. (2013)
2 more