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Publication Abstract from PubMed

alpha-1,3-Glucan is a homopolymer composed of D-glucose (Glc) and it is an extracellular polysaccharide found in dental plaque due to Streptococcus species. alpha-1,3-Glucanase from Streptomyces thermodiastaticus strain HF3-3 (Agl-ST) has been identified as a thermostable alpha-1,3-glucanase, which is classified into glycoside hydrolase family 87 (GH87) and specifically hydrolyzes alpha-1,3-glucan with an endo-action. The enzyme has a potential to inhibit the production of dental plaque and to be used for biotechnological applications. Here we show the structure of the catalytic unit of Agl-ST determined at 1.16 A resolution using X-ray crystallography. The catalytic unit is composed of two modules, a beta-sandwich fold module, and a right-handed beta-helix fold module, which resembles other structural characterized GH87 enzymes from Bacillus circulans str. KA-304 and Paenibacillus glycanilyticus str. FH11, with moderate sequence identities between each other (approximately 27% between the catalytic units). However, Agl-ST is smaller in size and more thermally stable than the others. A disulfide bond that anchors the C-terminal coil of the beta-helix fold, which is expected to contribute to thermal stability only exists in the catalytic unit of Agl-ST.

Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3.,Itoh T, Panti N, Hayashi J, Toyotake Y, Matsui D, Yano S, Wakayama M, Hibi T Biochem Biophys Res Commun. 2020 Oct 8. pii: S0006-291X(20)31894-5. doi:, 10.1016/j.bbrc.2020.09.133. PMID:33041007^[1]

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