The structure of cucurbitin: subunit symmetry and organization in situ.
The low-resolution (2 nm) subunit symmetry of cucurbitin, the crystalline seed storage globulin of cucurbits, has been determined by X-ray diffraction. The wet crystals belong to the cubic space group F23 and there are 4 molecules per unit cell. The molecules therefore possess point-group symmetry 23 and contain 12 structural units which at this resolution are indistinguishable. On drying, the crystal lattice dimension shrinks from 13.6 nm to 12.4 nm with no apparent change in symmetry. Diffraction patterns of small crystals spun into a pellet, and sections of dry and wet native seed indicate that in situ the protein is organised in microcrystals of the same unit cell and symmetry. Edestin, the crystalline storage globulin from cannabis, and a crystalline globulin from tobacco seed both have the same crystal lattice as cucurbitin and, very likely, the same subunit symmetry.
D003460:Crystallization; D005916:Globulins; D046911:Macromolecular Substances; D010940:Plant Proteins; D011487:Protein Conformation; D012639:Seeds / Q000032:analysis*; D014961:X-Ray Diffraction
D005916:Globulins; D046911:Macromolecular Substances; D010940:Plant Proteins