Crystal structure of soybean proglycinin alaB1b homotrimer

Soybean glycinin is a member of the 11 S globulin family. The crystal struc ture of proglycinin was determined by X-ray crystallography at 2.8 Angstrom resolution with an R-factor of 0.199 and a free X-factor of 0.250. A trime r molecule was found in an asymmetric unit of crystals. The trimer model co ntains three A1aB1b subunits and comprises 1128 amino acid residues and 34 water molecules. The constituent protomers of the homo-trimeric protein are arranged around a 3-fold symmetry axis with dimensions of 95 Angstrom x 95 Angstrom x 40 A. The protomer model is composed of five fragments which co rrespond roughly to conserved regions based on the sequence alignment of va rious 11 S globulins. The core of the protomer consists of two jelly-roll b eta -barrels and two extended helix domains. This structure of proglycinin is similar to those of canavalin and phaseolin belonging to the 7 S globuli n family, strongly supporting the hypothesis that both 7 S and 11S globulin s are derived from a common ancestor. The inter and intra-chain disulfide b onds conserved in the 11S globulin family are clearly observed. It is found that the face with the inter-chain disulfide bond (IE face) contains more hydrophobic residues than that with the intra-chain disulfide bond. This su ggests that a mature hexamer is formed by the interaction between the IE fa ces after processing. (C) 2001 Academic Press.