title: Crystal structure of Sa240: a ribose pyranase homolog with partial active site from Staphylococcus aureus.
abstract: Ribose is transported into cells in its pyranose form and must be rearranged to its furanose form for further utilization. Ribose pyranase RbsD catalyzes the conversion of ribose from the pyranose to furanose form. This is the key step for substrate supply to ribokinase RbsK, which converts ribose to ribose-5-phosphate for further metabolism. Sequence analysis indicated Sa240 from Staphylococcus aureus was a ribose pyranase homolog. Here we showed that Sa240 formed dimeric structure both in solution and in crystal. S240-ribose complex structure showed a ribose binding site formed by an incomplete active site compared with RbsD. Because the catalytic activity of ribose pyranase depends on its oligomeric state, we propose Sa240 is catalytically inactive in its dimeric structure.
authors.affiliation: School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Ling
authors.initials: L
authors.lastname: Wang
authors.forename: Minhao
authors.initials: M
authors.lastname: Wu
authors.forename: Jianye
authors.initials: J
authors.lastname: Zang
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012266:Ribose / Q000737:chemistry*; D016415:Sequence Alignment; D013211:Staphylococcus aureus / Q000201:enzymology*; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; D012266:Ribose