8qqh

Structure of beta-galactosidase from Desulfurococcus amyloliticus

spinqualitylabelsall models 8qqh, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8qqh is a 2 chain structure with sequence from Desulfurococcus amylolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B8D3P7_DESA1 Publication Abstract from PubMed The most extensively studied beta-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 beta-galactosidase from the hyperthermophilic Thermoprotei archaeon Desulfurococcus amylolyticus (DabetaGal). Unlike fungal monomeric six-domain beta-galactosidases, the DabetaGal 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 beta-d-galactopyranosides, and its distinguishing feature is the ability to cleave pNP-beta-d-fucopyranoside. DabetaGal efficiently catalyzes the hydrolysis of lactose at high temperatures, remains stable and active at 65 degrees capital ES, Cyrillic, and retains activity at 95 degrees capital ES, Cyrillic with a half-life time value equal to 73 min. These properties make archaeal DabetaGal a more attractive candidate for biotechnology than the widely used fungal beta-galactosidases. The archaeal highly thermostable GH35 family beta-galactosidase DabetaGal has a unique seven domain protein fold.,Kil Y, Pichkur EB, Sergeev VR, Zabrodskaya Y, Myasnikov A, Konevega AL, Shtam T, Samygina VR, Rychkov GN FEBS J. 2024 Jun 2. doi: 10.1111/febs.17166. PMID:38825733 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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