Functional and Structural Analysis of a β-Glucosidase Involved in β-1,2-Glucan Metabolism in Listeria innocua

PloS One
Masahiro NakajimaHayao Taguchi

Abstract

Despite the presence of β-1,2-glucan in nature, few β-1,2-glucan degrading enzymes have been reported to date. Recently, the Lin1839 protein from Listeria innocua was identified as a 1,2-β-oligoglucan phosphorylase. Since the adjacent lin1840 gene in the gene cluster encodes a putative glycoside hydrolase family 3 β-glucosidase, we hypothesized that Lin1840 is also involved in β-1,2-glucan dissimilation. Here we report the functional and structural analysis of Lin1840. A recombinant Lin1840 protein (Lin1840r) showed the highest hydrolytic activity toward sophorose (Glc-β-1,2-Glc) among β-1,2-glucooligosaccharides, suggesting that Lin1840 is a β-glucosidase involved in sophorose degradation. The enzyme also rapidly hydrolyzed laminaribiose (β-1,3), but not cellobiose (β-1,4) or gentiobiose (β-1,6) among β-linked gluco-disaccharides. We determined the crystal structures of Lin1840r in complexes with sophorose and laminaribiose as productive binding forms. In these structures, Arg572 forms many hydrogen bonds with sophorose and laminaribiose at subsite +1, which seems to be a key factor for substrate selectivity. The opposite side of subsite +1 from Arg572 is connected to a large empty space appearing to be subsite +2 for the bind...Continue Reading

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Citations

Jun 14, 2019·Bioscience, Biotechnology, and Biochemistry·Kaito KobayashiHayao Taguchi
Apr 12, 2019·Nature Communications·Wenxia FangDaan M F van Aalten
Jan 30, 2020·Scientific Reports·Kazi Zubaida Gulshan AraEva Nordberg Karlsson

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Datasets Mentioned

BETA
AAB66561.1
AEE54288.1
AEW02328.1
EEV33587.1
ELK47769.1
ERI92988.1
ETT38232.1

Methods Mentioned

BETA
X-ray

Software Mentioned

Coot
Refmac5
MODEL
COFFEE
Grafit
SWISS
MOLREP

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