The first structure–function study of GH151 α‐ l ‐fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity

Koval'ová T, Kovaľ T, Stránský J, Kolenko P, Dušková J, Švecová L, Vodičková P, Spiwok V, Benešová E, Lipovová P, Dohnálek J
The FEBS Journal (2022 Feb 20)

doi: 10.1111/febs.16387 		Submitted to SASBDB: 2021 Jan 18
Published in SASBDB:

SASDKY7 – α-L-Fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus - wild type

Alpha-L-fucosidase experimental SAS data
OTHER model
Sample: Alpha-L-fucosidase tetramer, 297 kDa Paenibacillus thiaminolyticus (Bacillus … protein
Buffer: 50 mM potassium phosphate, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2019 Jul 16
RgGuinier 4.2 nm
Dmax 13.2 nm
VolumePorod 418 nm3

SASDKZ7 – α-L-Fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus - mutant H503A

Alpha-L-fucosidase H503A experimental SAS data
PYMOL model
Sample: Alpha-L-fucosidase H503A tetramer, 297 kDa Paenibacillus thiaminolyticus (Bacillus … protein
Buffer: 50 mM potassium phosphate, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2019 Jul 16
RgGuinier 4.5 nm
Dmax 13.5 nm
VolumePorod 433 nm3