Structural elucidation of dextran degradation mechanism by streptococcus mutans dextranase belonging to glycoside hydrolase family 66.

The Journal of Biological Chemistry
Nobuhiro SuzukiAtsuo Kimura

Abstract

Dextranase is an enzyme that hydrolyzes dextran α-1,6 linkages. Streptococcus mutans dextranase belongs to glycoside hydrolase family 66, producing isomaltooligosaccharides of various sizes and consisting of at least five amino acid sequence regions. The crystal structure of the conserved fragment from Gln(100) to Ile(732) of S. mutans dextranase, devoid of its N- and C-terminal variable regions, was determined at 1.6 Å resolution and found to contain three structural domains. Domain N possessed an immunoglobulin-like β-sandwich fold; domain A contained the enzyme's catalytic module, comprising a (β/α)(8)-barrel; and domain C formed a β-sandwich structure containing two Greek key motifs. Two ligand complex structures were also determined, and, in the enzyme-isomaltotriose complex structure, the bound isomaltooligosaccharide with four glucose moieties was observed in the catalytic glycone cleft and considered to be the transglycosylation product of the enzyme, indicating the presence of four subsites, -4 to -1, in the catalytic cleft. The complexed structure with 4',5'-epoxypentyl-α-d-glucopyranoside, a suicide substrate of the enzyme, revealed that the epoxide ring reacted to form a covalent bond with the Asp(385) side chain. T...Continue Reading

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Citations

May 21, 2013·Journal of Bacteriology·Krista M GiglioHolger Sondermann
Oct 24, 2015·Journal of Biochemistry·Nobuhiro SuzukiYoung-Min Kim
May 14, 2016·Bioscience, Biotechnology, and Biochemistry·Yoshifumi GozuTakashi Tonozuka
May 29, 2018·Bioscience, Biotechnology, and Biochemistry·Patcharapa KlahanAtsuo Kimura
Dec 3, 2014·The Journal of Biological Chemistry·Takayoshi TagamiAtsuo Kimura
Sep 17, 2021·Journal of Basic Microbiology·Zhe NingShujun Wang

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