Structural highlights
Publication Abstract from PubMed
Glycoside hydrolase (GH) 87-type alpha-1,3-glucanase hydrolyses the alpha-1,3-glucoside linkages of alpha-1,3-glucan, which is found in fungal cell walls and extracellular polysaccharides produced by oral Streptococci. In this study, we report on the molecular structure of the catalytic unit of GH 87-type alpha-1,3-glucanase, Agl-KA, from Bacillus circulans, as determined by x-ray crystallography at a resolution of 1.82 A. The catalytic unit constitutes a complex structure of two tandemly connected domains-the N-terminal galactose-binding-like domain and the C-terminal right-handed beta-helix domain. While the beta-helix domain is widely found among polysaccharide-processing enzymes, complex formation with the galactose-binding-like domain was observed for the first time. Biochemical assays showed that Asp1067, Asp1090 and Asp1091 are important for catalysis, and these residues are indeed located at the putative substrate-binding cleft, which forms a closed end and explains the product specificity.
Crystal structure of the catalytic unit of GH 87-type alpha-1,3-glucanase Agl-KA from Bacillus circulans.,Yano S, Suyotha W, Oguro N, Matsui T, Shiga S, Itoh T, Hibi T, Tanaka Y, Wakayama M, Makabe K Sci Rep. 2019 Oct 25;9(1):15295. doi: 10.1038/s41598-019-51822-5. PMID:31653959[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yano S, Suyotha W, Oguro N, Matsui T, Shiga S, Itoh T, Hibi T, Tanaka Y, Wakayama M, Makabe K. Crystal structure of the catalytic unit of GH 87-type alpha-1,3-glucanase Agl-KA from Bacillus circulans. Sci Rep. 2019 Oct 25;9(1):15295. doi: 10.1038/s41598-019-51822-5. PMID:31653959 doi:http://dx.doi.org/10.1038/s41598-019-51822-5
