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Structure paper

TitleStructure of a bacterial alpha-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases.
Journal, issue, pagesJ. Biol. Chem., Vol. 297, Page 101366-101366, Year 2021
Publish dateJul 19, 2021 (structure data deposition date)
AuthorsNakamura, S. / Nihira, T. / Kurata, R. / Nakai, H. / Funane, K. / Park, E.Y. / Miyazaki, T.
External linksJ. Biol. Chem. / PubMed:34728215
MethodsX-ray diffraction
Resolution1.4 - 1.54 Å
Structure data

PDB-7fe3:
Crystal structure of GH65 alpha-1,2-glucosidase from Flavobacterium johnsoniae
Method: X-RAY DIFFRACTION / Resolution: 1.54 Å

PDB-7fe4:
Crystal structure of GH65 alpha-1,2-glucosidase from Flavobacterium johnsoniae in complex with glucose
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-BGC:
beta-D-glucopyranose

Source
  • flavobacterium johnsoniae (strain atcc 17061 / dsm 2064 / jcm 8514 / nbrc 14942 / ncimb 11054 / uw101) (bacteria)
KeywordsHYDROLASE / Glycoside hydrolase / GH65 / (alpha/alpha)6-barrel / kojibiose / dextran

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