title: Automated docking of alpha-(1-->4)- and alpha-(1-->6)-linked glucosyl trisaccharides and maltopentaose into the soybean beta-amylase active site.
abstract: The Lamarckian genetic algorithm of AutoDock 3.0 was used to dock alpha-maltotriose, methyl alpha-panoside, methyl alpha-isopanoside, methyl alpha-isomaltotrioside, methyl alpha-(6(1)-alpha-glucopyranosyl)-maltoside, and alpha-maltopentaose into the closed and, except for alpha-maltopentaose, into the open conformation of the soybean beta-amylase active site. In the closed conformation, the hinged flap at the mouth of the active site closes over the substrate. The nonreducing end of alpha-maltotriose docks preferentially to subsites -2 or +1, the latter yielding nonproductive binding. Some ligands dock into less optimal conformations with the nonreducing end at subsite -1. The reducing-end glucosyl residue of nonproductively-bound alpha-maltotriose is close to residue Gln194, which likely contributes to binding to subsite +3. In the open conformation, the substrate hydrogen-bonds with several residues of the open flap. When the flap closes, the substrate productively docks if the nonreducing end is near subsites -2 or -1. Trisaccharides with alpha-(1-->6) bonds do not successfully dock except for methyl alpha-isopanoside, whose first and second glucosyl rings dock exceptionally well into subsites -2 and -1. The alpha-(1-->6) bond between the second and third glucosyl units causes the latter to be improperly positioned into subsite +1; the fact that isopanose is not a substrate of beta-amylase indicates that binding to this subsite is critical for hydrolysis.
authors.affiliation: Department of Chemical Engineering, Iowa State University, Ames 50011- 2230, USA.
authors.forename: W M
authors.initials: WM
authors.lastname: Rockey
authors.forename: A
authors.initials: A
authors.lastname: Laederach
authors.forename: P J
authors.initials: PJ
authors.lastname: Reilly
mesh_terms: D000465:Algorithms; D001665:Binding Sites; D003198:Computer Simulation; D008320:Maltose / Q000378:metabolism; D008958:Models, Molecular; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D012984:Software; D013025:Glycine max / Q000201:enzymology*; D014312:Trisaccharides / Q000737:chemistry / Q000378:metabolism*; D001614:beta-Amylase / Q000737:chemistry*
chemical_list: D009844:Oligosaccharides; D014312:Trisaccharides; C019193:maltopentaose; C008317:maltotriose; D008320:Maltose; D001614:beta-Amylase