title: Some observations of a correlation between the symmetry of large heavy-atom complexes and their binding sites on proteins.
abstract: Two large, electron dense heavy-metal complexes were found to bind to crystals of heavy riboflavin synthase. The crystallographic analysis by difference Fourier methods shows that the tungsten cluster compound [(W3O2(O2CCH3)6]2+, which has trigonal symmetry, binds to a site on the 3-fold axis of the protein. The heteropolytungstate compound [NaP5W30O110]14-, which has pentagonal symmetry, binds to a site on the 5-fold axis of the protein.
authors: Max-Planck-Institut für Biochemie, Martinsried, F.R.G.
authors: R
authors: R
authors: Ladenstein
authors: A
authors: A
authors: Bacher
authors: R
authors: R
authors: Huber
mesh_terms: D001665:Binding Sites; D003461:Crystallography; D012258:Riboflavin Synthase; D014166:Transferases
chemical_list: D014166:Transferases; D012258:Riboflavin Synthase