title: Interdomain disulfide bridge in the rice granule bound starch synthase I catalytic domain as elucidated by X-ray structure analysis.
abstract: The catalytic domain of rice (Oryza sativa japonica) granule bound starch synthase I (OsGBSSI-CD) was overexpressed and the three-dimensional structures of the ligand-free and ADP-bound forms were determined. The structures were similar to those reported for bacterial and archaeal glycogen synthases, which belong to glycosyltransferase family 5. They had Rossmann fold N- and C-domains connected by canonical two-hinge peptides, and an interdomain disulfide bond that appears to be conserved in the Poaceae plant family. The presence of three covalent linkages might explain why both OsGBSSI-CD structures adopted only the closed domain arrangement.
authors.affiliation: Biomolecular Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan. momma@affrc.go.jp
authors.forename: Mitsuru
authors.initials: M
authors.lastname: Momma
authors.forename: Zui
authors.initials: Z
authors.lastname: Fujimoto
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004220:Disulfides / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006006:Glycogen Synthase / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012275:Oryza / Q000737:chemistry* / Q000201:enzymology; D010802:Phylogeny; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013214:Starch Synthase / Q000737:chemistry* / Q000235:genetics
chemical_list: D004220:Disulfides; D010940:Plant Proteins; D011994:Recombinant Proteins; C434607:granule-bound starch synthase I; D006006:Glycogen Synthase; D013214:Starch Synthase