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X-ray diffraction
2Å resolution

Microbacterium saccharophilum K-1 beta-fructofuranosidase mutant T47S/S200T/F447V/P500S

Released:
DOI: 10.2210/pdb3wpy/pdb
PDB entry 3wpy coloured by chain, front view.
PDB entry 3wpy coloured by chain, side view.
PDB entry 3wpy coloured by chain, top view.
Source organism: Microbacterium saccharophilum
Primary publication:
Enhancing thermostability and the structural characterization of Microbacterium saccharophilum K-1 β-fructofuranosidase.
Ohta Y, Hatada Y, Hidaka Y, Shimane Y, Usui K, Ito T, Fujita K, Yokoi G, Mori M, Sato S, Miyazaki T, Nishikawa A, Tonozuka T
Appl Microbiol Biotechnol 98 6667-77 (2014)
PMID: 24633372

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase family 68 protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 542 amino acids
Theoretical weight: 59.36 KDa
Source organism: Microbacterium saccharophilum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8VW87 (Residues: 37-578; Coverage: 100%)
Gene names: FVP74_04720, bff
Sequence domains: Levansucrase/Invertase
Structure domains: Glycosyl hydrolase domain; family 43

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P1
Unit cell:
a: 57.238Å b: 81.714Å c: 90.962Å
α: 66.85° β: 87.11° γ: 88.48°
R-values:
R R work R free
0.196 0.193 0.246
Expression system: Escherichia coli

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Citations

1 review citation

Recent novel applications of levansucrases.
Li et al. (2015)
8 other articles