7C7D

Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3

Summary for 7C7D

• Entry DOI: 10.2210/pdb7c7d/pdb
• Descriptor: alpha-1,3-glucanase, CALCIUM ION, PENTAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: glycosidase, hydrolase
• Biological source: Streptomyces thermodiastaticus
• Total number of polymer chains: 2
• Total formula weight: 126870.70

Authors

Itoh, T.,Panti, N.,Toyotake, Y.,Hayashi, J.,Suyotha, W.,Yano, S.,Wakayama, M.,Hibi, T. (deposition date: 2020-05-25, release date: 2020-11-11, Last modification date: 2024-11-06)

Primary citation

Itoh, T.,Panti, N.,Hayashi, J.,Toyotake, Y.,Matsui, D.,Yano, S.,Wakayama, M.,Hibi, T.
Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3.
Biochem.Biophys.Res.Commun., 533:1170-1176, 2020

PubMed Abstract: α-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. α-1,3-Glucanase from Streptomyces thermodiastaticus strain HF3-3 (Agl-ST) has been identified as a thermostable α-1,3-glucanase, which is classified into glycoside hydrolase family 87 (GH87) and specifically hydrolyzes α-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 Å resolution using X-ray crystallography. The catalytic unit is composed of two modules, a β-sandwich fold module, and a right-handed β-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 β-helix fold, which is expected to contribute to thermal stability only exists in the catalytic unit of Agl-ST.

PubMed: 33041007
DOI: 10.1016/j.bbrc.2020.09.133

Experimental method

X-RAY DIFFRACTION (1.16 Å)