EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	A disulfide redox switch mechanism regulates glycoside hydrolase function.
ジャーナル・号・ページ	Nat Commun, Vol. 17, Issue 1, Page 45, Year 2026
掲載日	2026年1月5日
著者	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 要旨	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.
リンク	Nat Commun / PubMed:41491304 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	2 - 3.41 Å
構造データ	EMDB-49363: Cryo-EM map of the inactive conformation of a glycoside hydrolase (CapGH2b) from the GH2 family 手法: EM (単粒子) / 解像度: 3.41 Å 49364 9nfe EMDB-49364, PDB-9nfe: Active conformation of a redox-regulated glycoside hydrolase (CapGH2b) from the GH2 family 手法: EM (単粒子) / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 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 手法: X-RAY DIFFRACTION / 解像度: 3.1 Å
化合物	ChemComp-PO4: PHOSPHATE ION ChemComp-GOL: GLYCEROL ChemComp-HOH: WATER ChemComp-TAU: 2-AMINOETHANESULFONIC ACID ChemComp-PEG: DI(HYDROXYETHYL)ETHER ChemComp-PG4: TETRAETHYLENE GLYCOL / 沈殿剤YM ChemComp-ACT: ACETATE ION ChemComp-MLI: MALONATE ION ChemComp-EDO*: 1,2-ETHANEDIOL
由来	metagenome (メタゲノム)
キーワード	HYDROLASE / redox-regulation / glycosyl hydrolase / mannosidase / redox-switch / metagenome / disulfide bond