Crystal structure of the GH-46 subclass III chitosanase from Bacillus circulans MH-K1 in complex with chitotetraose

CONCLUSIONS: Although GH-46 chitosanases vary in the finer details of the subsites defining cleavage specificity, they share similar structural characteristics in substrate-binding, catalytic processes, and potentially in conformational change.GENERAL SIGNIFICANCE: The precise binding of a GlcN residue to the -2 subsite is essential for the conformational shift that occurs in all GH-46 chitosanases, as shown by the crystal structures of the apo- and substrate-bound forms of MH-K1 chitosanase.PMID:38158023 | DOI:10.1016/j.bbagen.2023.130549

Source: Biochimica et Biophysica Acta - December 29, 2023 Category: Biochemistry Authors: Michihiko Suzuki Akihiro Saito Mariko Kobayashi Tomofumi Yokoyama Shoko Omiya Jian Li Kei Sugita Kunio Miki Jun-Ichi Saito Akikazu Ando Source Type: research