8QQH

Structure of beta-galactosidase from Desulfurococcus amyloliticus

This is a non-PDB format compatible entry.

Summary for 8QQH

• Entry DOI: 10.2210/pdb8qqh/pdb
• Descriptor: Beta-galactosidase (2 entities in total)
• Functional Keywords: beta-galactosidase, hydrolase
• Biological source: Desulfurococcus amylolyticus
• Total number of polymer chains: 2
• Total formula weight: 226490.58

Authors

Samygina, V.R.,Kil, Y.,Sergeev, R.S.,Rychkov, G.N. (deposition date: 2023-10-04, release date: 2024-08-14, Last modification date: 2024-11-06)

Primary citation

Kil, Y.,Pichkur, E.B.,Sergeev, V.R.,Zabrodskaya, Y.,Myasnikov, A.,Konevega, A.L.,Shtam, T.,Samygina, V.R.,Rychkov, G.N.
The archaeal highly thermostable GH35 family beta-galactosidase Da beta Gal has a unique seven domain protein fold.
Febs J., 291:3686-3705, 2024

PubMed Abstract: The most extensively studied β-d-galactosidases (EC3.2.1.23) belonging to four glycoside hydrolase (GH) families 1, 2, 35, and 42 are widely distributed among Bacteria, Archaea and Eukaryotes. Here, we report a novel GH35 family β-galactosidase from the hyperthermophilic Thermoprotei archaeon Desulfurococcus amylolyticus (DaβGal). Unlike fungal monomeric six-domain β-galactosidases, the DaβGal enzyme is a dimer; it has an extra jelly roll domain D7 and three composite domains (D4, D5, and D6) that are formed by the distantly located polypeptide chain regions. The enzyme possesses a high specificity for β-d-galactopyranosides, and its distinguishing feature is the ability to cleave pNP-β-d-fucopyranoside. DaβGal efficiently catalyzes the hydrolysis of lactose at high temperatures, remains stable and active at 65 °С, and retains activity at 95 °С with a half-life time value equal to 73 min. These properties make archaeal DaβGal a more attractive candidate for biotechnology than the widely used fungal β-galactosidases.

PubMed: 38825733
DOI: 10.1111/febs.17166

Experimental method

X-RAY DIFFRACTION (2.15 Å)