Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structures of human fucosidase FucA1 reveal insight into substrate recognition and catalysis.
Journal, issue, pages	Structure, Vol. 30, Issue 10, Page 1443-11451.e5, Year 2022
Publish date	Oct 6, 2022
Authors	Zachary Armstrong / Richard W Meek / Liang Wu / James N Blaza / Gideon J Davies /
PubMed Abstract	Enzymatic 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 links	Structure / PubMed:35907402 / PubMed Central
Methods	EM (single particle)
Resolution	2.49 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 / N-Acetylglucosamine ChemComp-HOH: WATER / Water ChemComp-DFU: (2S,3R,4S,5R)-2-METHYLPIPERIDINE-3,4,5-TRIOL
Source	homo sapiens (human)
Keywords	HYDROLASE / Fucosidase