Structural and biochemical characterization of fructose-1,6/sedoheptulose-1,7-bisphosphatase from the cyanobacterium Synechocystis strain 6803
Cyanobacterial fructose-1,6/sedoheptulose-1,7-bisphosphatase (cy-FBP/SBPase) plays a vital role in gluconeogenesis and in the photosynthetic carbon reduction pathway, and is thus a potential enzymatic target for inhibition of harmful cyanobacterial blooms.Here, we describe the crystal structure of cy-FBP/SBPase in complex with AMP and fructose-1,6-bisphosphate (FBP).The allostenc inhibitor AMP and the substrate FBP exhibit an unusual binding mode when in complex with cy-FBP/SBPase.Binding mode analysis suggested that AMP bound to the allosteric sites near the interface across the up/down subunit pairs C1C4 and C2C3 in the center of the tetramer, while FBP binds opposite to the interface between the horizontal subunit pairs C1C2 or C3C4.We identified a series of residues important for FBP and AMP binding, and suggest formation of a disulfide linkage between Cys75 and Cys99.Further analysis indicates that cy-FBP/ SBPase may be regulated through ligand binding and alteration of the structure of the enzyme complex.The interactions between ligands and cy-FBP/SBPase are different from those of hgand-bound structures of other FBPase family members, and thus provide new insight into the molecular mechanisms of structure and catalysis of cy-FBP/SBPase.Our studies provide insight into the evolution of this enzyme family, and may help in the design ofinhibitors aimed at preventing toxic cyanobactenal blooms.
biochemical characterization cyanobacteria fructose 1,6/sedoheptulose 1,7 bisphosphatase,site directed mutagenesis structure
Lingling Feng Xiaopeng Hu Yao Sun Hui Deng Ding Li Jian Wan Xiaofeng Wang Weiwei Wang Xun Liao Yanliang Ren
Key Laboratory of Pesticide & Chemical Biology (CCNU), Ministry of Education, and College of Chemist School of Pharmaceutical Science, Sun Yat-sen University, Guangzhou, China
国内会议
苏州
英文
359-369
2014-10-26（万方平台首次上网日期，不代表论文的发表时间）