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	A disulfide redox switch mechanism regulates glycoside hydrolase function.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Page 45, Year 2026
Publish date	Jan 5, 2026
Authors	Marcele Pandeló Martins / Gustavo Henrique Martins / Felipe Jun Fuzita / João Paulo Menezes Spadeto / Renan Yuji Miyamoto / Felippe Mariano Colombari / Fabiane Stoffel / Luciano Graciani Dolce / Camila Ramos Dos Santos / Rodrigo Silva Araujo Streit / Antônio Carlos Borges / Rafael Henrique Galinari / Yoshihisa Yoshimi / Paul Dupree / Gabriela Felix Persinoti / Mariana Abrahão Bueno Morais / Mario Tyago Murakami /
PubMed Abstract	Disulfide bonds are a key post-translational modification involved in protein folding, structural stability, and functional regulation. Here, we demonstrate that a glycoside hydrolase from the GH2 ...Disulfide bonds are a key post-translational modification involved in protein folding, structural stability, and functional regulation. Here, we demonstrate that a glycoside hydrolase from the GH2 family undergoes reversible redox regulation through an intramolecular disulfide bond. The enzyme is inactive in its oxidized state and becomes active when reduced through a fully reversible process. Under oxidative conditions, multiple crystallographic and cryo-EM structures revealed a pronounced structural disorder in the active site, most prominent in the regulatory and catalytic loops, which disrupts the substrate binding site and, remarkably, the configuration of the acidic catalytic residues. Conversely, a high-resolution cryo-EM structure of the active (reduced) state unveiled a well-ordered active site with catalytic residues properly positioned for a classical Koshland retaining mechanism. This reversible order-disorder process based on a disulfide switch provides a mechanism for redox-dependent control of glycoside hydrolase activity, with potential implications for carbohydrate metabolism, microbial adaptation and biotechnological applications.
External links	Nat Commun / PubMed:41491304 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2 - 3.41 Å
Structure data	EMDB-49363: Cryo-EM map of the inactive conformation of a glycoside hydrolase (CapGH2b) from the GH2 family Method: EM (single particle) / Resolution: 3.41 Å 49364 9nfe EMDB-49364, PDB-9nfe: Active conformation of a redox-regulated glycoside hydrolase (CapGH2b) from the GH2 family Method: EM (single particle) / Resolution: 2.62 Å PDB-9np8: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b) from the GH2 family in the space group I213 at 2.05 A Method: X-RAY DIFFRACTION / Resolution: 2 Å PDB-9np9: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b - E553Q Mutant) from the GH2 family in the space group I213 at 2.6 A Method: X-RAY DIFFRACTION / Resolution: 2.6 Å PDB-9npa: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b) from the GH2 family in the space group I213 at 2.75 A Method: X-RAY DIFFRACTION / Resolution: 2.75 Å PDB-9npb: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b) from the GH2 family in the space group R3 at 2.45 A Method: X-RAY DIFFRACTION / Resolution: 2.45 Å PDB-9npc: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b) from the GH2 family in the space group I212121 at 2.65 A Method: X-RAY DIFFRACTION / Resolution: 2.65 Å PDB-9npd: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b - E553Q Mutant) from the GH2 family in the space group P3121 at 3.05 A Method: X-RAY DIFFRACTION / Resolution: 3.05 Å PDB-9npe: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b) from the GH2 family in the space group P1 at 2.40 A Method: X-RAY DIFFRACTION / Resolution: 2.4 Å PDB-9npf: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b) from the GH2 family in the space group P1 at 2.15 A Method: X-RAY DIFFRACTION / Resolution: 2.15 Å PDB-9npl: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b - E553Q Mutant) from the GH2 family in the space group P1 at 2.25 A Method: X-RAY DIFFRACTION / Resolution: 2.25 Å PDB-9npn: Crystal structure of the inactive conformation of a glycoside hydrolase (CapGH2b - E465A Mutant) from the GH2 family in the space group P1 at 3.1 A Method: X-RAY DIFFRACTION / Resolution: 3.1 Å
Chemicals	ChemComp-PO4: PHOSPHATE ION ChemComp-GOL: GLYCEROL ChemComp-HOH: WATER ChemComp-TAU: 2-AMINOETHANESULFONIC ACID ChemComp-PEG: DI(HYDROXYETHYL)ETHER ChemComp-PG4: TETRAETHYLENE GLYCOL / precipitantYM ChemComp-ACT: ACETATE ION ChemComp-MLI: MALONATE ION ChemComp-EDO*: 1,2-ETHANEDIOL
Source	metagenome (others)
Keywords	HYDROLASE / redox-regulation / glycosyl hydrolase / mannosidase / redox-switch / metagenome / disulfide bond