3TA9

beta-Glucosidase A from the halothermophile H. orenii

Summary for 3TA9

• Entry DOI: 10.2210/pdb3ta9/pdb
• Descriptor: Glycoside hydrolase family 1, NICKEL (II) ION (3 entities in total)
• Functional Keywords: tim barrel, glucosidase, hydrolase
• Biological source: Halothermothrix orenii
• Total number of polymer chains: 2
• Total formula weight: 106434.45

Authors

Hofmann, A.,Wang, C.K.,Kori, L.D.,Patel, B.K. (deposition date: 2011-08-03, release date: 2012-02-22, Last modification date: 2023-09-13)

Primary citation

Kori, L.D.,Hofmann, A.,Patel, B.K.
Expression, purification and preliminary crystallographic analysis of the recombinant (beta)-glucosidase (BglA) from the halothermophile Halothermothrix orenii
Acta Crystallogr.,Sect.F, 67:111-113, 2011

PubMed Abstract: The β-glucosidase A gene (bglA) has been cloned from the halothermophilic bacterium Halothermothrix orenii and the recombinant enzyme (BglA; EC 3.2.1.21) was bacterially expressed, purified using metal ion-affinity chromatography and subsequently crystallized. Orthorhombic crystals were obtained that diffracted to a resolution limit of 3.5 Å. The crystal structure with two molecules in the asymmetric unit was solved by molecular replacement using a library of known glucosidase structures. Attempts to collect higher resolution diffraction data from crystals grown under different conditions and structure refinement are currently in progress.

PubMed: 21206038
DOI: 10.1107/S1744309110046981

Experimental method

X-RAY DIFFRACTION (3 Å)