› 5hvl

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-187661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] Chains: A, B
Molecule details ›
Chains: A, B
Length: 478 amino acids
Theoretical weight: 54.52 KDa
Source organism: Candida albicans SC5314
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q92410 (Residues: 1-478; Coverage: 100%)
Gene names: CAALFM_CR05720WA, CaO19.13961, CaO19.6640, TPS1
Sequence domains: Glycosyltransferase family 20
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

3 bound ligands:
Ligand UDP 2 x UDP
Ligand VDM 2 x VDM
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6522
Unit cell:
a: 115.563Å b: 115.563Å c: 282.69Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.179 0.206
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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Citations

2 review citations

An insight into new strategies to combat antifungal drug resistance.
Zheng et al. (2018)
1 more

1 mention without citation

Structural and In Vivo Studies on Trehalose-6-Phosphate Synthase from Pathogenic Fungi Provide Insights into Its Catalytic Mechanism, Biological Necessity, and Potential for Novel Antifungal Drug Design.
Miao et al. (2017)