3WQ8

Monomer structure of hyperthermophilic beta-glucosidase mutant forming a dodecameric structure in the crystal form

Summary for 3WQ8

• Entry DOI: 10.2210/pdb3wq8/pdb
• Related: 3APG 3WDP
• Descriptor: Beta-glucosidase (2 entities in total)
• Functional Keywords: tim barrel, hydrolase, sugar binding, hydrolysis
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 12
• Total formula weight: 622339.97

Authors

Nakabayashi, M.,Kataoka, M.,Watanabe, M.,Ishikawa, K. (deposition date: 2014-01-23, release date: 2014-07-09, Last modification date: 2023-11-08)

Primary citation

Nakabayashi, M.,Kataoka, M.,Watanabe, M.,Ishikawa, K.
Monomer structure of a hyperthermophilic beta-glucosidase mutant forming a dodecameric structure in the crystal form.
Acta Crystallogr.,Sect.F, 70:854-859, 2014

PubMed Abstract: One of the β-glucosidases from Pyrococcus furiosus (BGLPf) is found to be a hyperthermophilic tetrameric enzyme that can degrade cellooligosaccharides. Recently, the crystal structures of the tetrameric and dimeric forms were solved. Here, a new monomeric form of BGLPf was constructed by removing the C-terminal region of the enzyme and its crystal structure was solved at a resolution of 2.8 Å in space group P1. It was discovered that the mutant enzyme forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal. Under biological conditions, the mutant enzyme forms a monomer. This result helps explain how BGLPf has attained its oligomeric structure and thermostability.

PubMed: 25005077
DOI: 10.1107/S2053230X14010188

Experimental method

X-RAY DIFFRACTION (2.81 Å)