3wq8

Publication Abstract from PubMed

One of the beta-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 A 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.

Monomer structure of a hyperthermophilic beta-glucosidase mutant forming a dodecameric structure in the crystal form.,Nakabayashi M, Kataoka M, Watanabe M, Ishikawa K Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):854-9. doi:, 10.1107/S2053230X14010188. Epub 2014 Jun 18. PMID:25005077^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.