An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase.

Bishnoi, Ritika and Mahajan, Sonal and Ramya, T N C (2018) An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase. Glycobiology, 28 (11). pp. 860-875. ISSN 1460-2423

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Official URL: https://academic.oup.com/glycob/article/28/11/860/...

Abstract

F-type lectins are phylogenetically widespread but selectively distributed fucose-binding lectins with L-fucose- and calcium-binding sequence motifs and an F-type lectin fold. Bacterial F-type lectin domains frequently occur in tandem with various protein domains in diverse architectures, indicating a possible role in directing enzyme activities or other biological functions to distinct fucosylated niches. Here, we report the biochemical characterization of a Streptosporangium roseum protein containing an F-type lectin domain in tandem with an NPCBM-associated domain and a family GH 29A alpha-l-fucosidase domain. We show that the F-type lectin domain of this protein recognizes fucosylated glycans in both α and β linkages but has high affinity for a Fuc-α-1,2-Gal motif and that the alpha-l-fucosidase domain displays hydrolytic activity on glycan substrates with α1-2 and α1-4 linked fucose. We also show that the F-type lectin domain does not have any effect on the activity of the cis-positioned alpha-l-fucosidase domain with the synthetic substrate, 4-Methylumbelliferyl-alpha-l-fucopyranoside or on inhibition of this activity by l-fucose or deoxyfuconojirimycin hydrochloride. However, the F-type lectin domain together with the NPCBM-associated domain enhances the activity of the cis-positioned alpha-l-fucosidase domain for soluble fucosylated oligosaccharide substrates. While there are many reports of glycoside hydrolase activity towards insoluble and soluble polysaccharides being enhanced by cis-positioned carbohydrate binding modules on the polypeptide, this is the first report, to our knowledge, of enhancement of activity towards aqueous, freely diffusible, small oligosaccharides. We propose a model involving structural stabilization and a bind-and-jump action mediated by the F-type lectin domain to rationalize our findings.

Item Type: Article
Additional Information: Copyright of this article belongs to OUP.
Uncontrolled Keywords: alpha-L-fucosidase; carbohydrate-binding module; F-type lectin domain; fucose; Streptosporangium roseum
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 19 Mar 2019 09:28
Last Modified: 19 Mar 2019 09:28
URI: http://crdd.osdd.net/open/id/eprint/2150

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