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TitleCryo-EM structures of human fucosidase FucA1 reveal insight into substrate recognition and catalysis.
Journal, issue, pagesStructure, Vol. 30, Issue 10, Page 1443-11451.e5, Year 2022
Publish dateOct 6, 2022
AuthorsZachary Armstrong / Richard W Meek / Liang Wu / James N Blaza / Gideon J Davies /
PubMed AbstractEnzymatic hydrolysis of α-L-fucose from fucosylated glycoconjugates is consequential in bacterial infections and the neurodegenerative lysosomal storage disorder fucosidosis. Understanding human α- ...Enzymatic hydrolysis of α-L-fucose from fucosylated glycoconjugates is consequential in bacterial infections and the neurodegenerative lysosomal storage disorder fucosidosis. Understanding human α-L-fucosidase catalysis, in an effort toward drug design, has been hindered by the absence of three-dimensional structural data for any animal fucosidase. Here, we have used cryoelectron microscopy (cryo-EM) to determine the structure of human lysosomal α-L-fucosidase (FucA1) in both an unliganded state and in complex with the inhibitor deoxyfuconojirimycin. These structures, determined at 2.49 Å resolution, reveal the homotetrameric structure of FucA1, the architecture of the catalytic center, and the location of both natural population variations and disease-causing mutations. Furthermore, this work has conclusively identified the hitherto contentious identity of the catalytic acid/base as aspartate-276, representing a shift from both the canonical glutamate acid/base residue and a previously proposed glutamate residue. These findings have furthered our understanding of how FucA1 functions in both health and disease.
External linksStructure / PubMed:35907402 / PubMed Central
MethodsEM (single particle)
Resolution2.49 Å
Structure data

13499

7pls

EMDB-13499, PDB-7pls:
Cryo-EM structures of human fucosidase FucA1 reveal insight into substate recognition and catalysis.
Method: EM (single particle) / Resolution: 2.49 Å

13520

7pm4

EMDB-13520, PDB-7pm4:
Cryo-EM structures of human fucosidase FucA1 reveal insight into substate recognition and catalysis.
Method: EM (single particle) / Resolution: 2.49 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-DFU:
(2S,3R,4S,5R)-2-METHYLPIPERIDINE-3,4,5-TRIOL

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Fucosidase

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