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TitleThe first structure-function study of GH151 alpha-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity
Journal, issue, pagesFebs J., Year 2022
Publish dateJan 9, 2020 (structure data deposition date)
AuthorsKoval'ova, T. / Koval, T. / Stransky, J. / Kolenko, P. / Duskova, J. / Svecova, L. / Vodickova, P. / Spiwok, V. / Benesova, E. / Lipovova, P. / Dohnalek, J.
External linksFebs J. / Search PubMed
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-6tvk:
Alpha-L-fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-TBR:
HEXATANTALUM DODECABROMIDE

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • paenibacillus thiaminolyticus (bacteria)
KeywordsHYDROLASE / ALPHA-L-FUCOSIDASE / GH151 / ACTIVE SITE COMPLEMENTATION / TETRAMER

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