2.4.1.281 | to 1.68 A resolution. The enzyme shows a homohexameric structure, which is formed by using two helices attached to the N-terminus and C-terminus as a tab for sticking between subunits. In complexes with substrates, 4-O-beta-D-mannosyl-D-glucose and phosphate, and the product D-mannose-1-phosphate the structures reveal that the invariant residue Asp131, is supposed to be the general acid/base, does not exist close to the glycosidic Glc-O4 atom, which should be protonated in the catalytic reaction |
736635 |