Monomer structure of a hyperthermophilic β-glucosidase mutant forming a dodecameric structure in the crystal form
2014 ◽
Vol 70
(7)
◽
pp. 854-859
Keyword(s):
One of the β-glucosidases fromPyrococcus 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 groupP1. 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.
2015 ◽
Vol 71
(10)
◽
pp. 1117-1120
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Keyword(s):
1988 ◽
Vol 43
(1)
◽
pp. 5-11
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Keyword(s):
2021 ◽
Vol 77
(9)
◽
2000 ◽
Vol 55
(9-10)
◽
pp. 791-800
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Keyword(s):
Keyword(s):
2004 ◽
Vol 60
(1)
◽
pp. 90-96
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2006 ◽
Vol 61
(10-11)
◽
pp. 588-594
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Keyword(s):
Keyword(s):