5ZRU

Crystal structure of Agl-KA catalytic domain

Summary for 5ZRU

• Entry DOI: 10.2210/pdb5zru/pdb
• Descriptor: Alpha-1,3-glucanase, 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL, SULFATE ION, ... (6 entities in total)
• Functional Keywords: agl-ka gh87, hydrolase
• Biological source: Bacillus circulans
• Total number of polymer chains: 2
• Total formula weight: 126342.20

Authors

Yano, S.,Makabe, K. (deposition date: 2018-04-25, release date: 2019-10-23, Last modification date: 2024-03-27)

Primary citation

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, 9:15295-15295, 2019

PubMed Abstract: Glycoside hydrolase (GH) 87-type α-1,3-glucanase hydrolyses the α-1,3-glucoside linkages of α-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 α-1,3-glucanase, Agl-KA, from Bacillus circulans, as determined by x-ray crystallography at a resolution of 1.82 Å. 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 β-helix domain. While the β-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.

PubMed: 31653959
DOI: 10.1038/s41598-019-51822-5

Experimental method

X-RAY DIFFRACTION (1.833 Å)