Heavy riboflavin synthase from Bacillus subtilis. Crystal structure analysis of the icosahedral beta 60 capsid at 3.3 A resolution.
Geometric features as well as possible functional properties of the substrate binding sites at the pentamer interfaces are described. Ligand binding at the pentamer interface regions increases the stability of the beta 60 capsid considerably and influences the reassembly of isolated beta-subunits.
Ladenstein
R
R
Max-Planck-Institut für Biochemie Martinsried, F.R.G.
Schneider
M
M
Huber
R
R
Bartunik
H D
HD
Wilson
K
K
Schott
K
K
Bacher
A
A
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D002213:Capsid; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012256:Riboflavin / Q000096:biosynthesis; D012258:Riboflavin Synthase / Q000378:metabolism; D014166:Transferases / Q000378:metabolism; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D014166:Transferases; D012258:Riboflavin Synthase; D012256:Riboflavin