title: Structure of glyceraldehyde-3-phosphate dehydrogenase from the archaeal hyperthermophile Methanocaldococcus jannaschii.
abstract: The X-ray crystal structure of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the hyperthermophilic archaeon Methanocaldococcus jannaschii (Mj-GAPDH) was determined to 1.81 A resolution. The crystal belonged to space group C222(1), with unit-cell parameters a = 83.4, b = 152.0, c = 118.6 A. The structure was solved by molecular replacement and was refined to a final R factor of 17.1% (R(free) = 19.8%). The final structure included the cofactor NADP(+) at the nucleotide-binding site and featured unoccupied inorganic and substrate phosphate-binding sites. A comparison with GAPDH structures from mesophilic sources suggested that Mj-GAPDH is stabilized by extensive electrostatic interactions between the C-terminal alpha-helices and various distal loop regions, which are likely to contribute to thermal stability. The key phosphate-binding residues in the active site of Mj-GAPDH are conserved in other archaeal GAPDH proteins. These residues undergo a conformational shift in response to occupancy of the inorganic phosphate site.
authors.affiliation: Systems and Structural Biology Center, Yokohama Institute, RIKEN, 1-7-22 Suehiro, Tsurumi, Yokohama 230-0045, Japan.
authors.forename: Ali D
authors.initials: AD
authors.lastname: Malay
authors.forename: Yoshitaka
authors.initials: Y
authors.lastname: Bessho
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Ellis
authors.forename: Svetlana V
authors.initials: SV
authors.lastname: Antonyuk
authors.forename: Richard W
authors.initials: RW
authors.lastname: Strange
authors.forename: S Samar
authors.initials: SS
authors.lastname: Hasnain
authors.forename: Akeo
authors.initials: A
authors.lastname: Shinkai
authors.forename: Balasundaram
authors.initials: B
authors.lastname: Padmanabhan
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D019766:Genes, Archaeal; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / Q000737:chemistry* / Q000235:genetics; D017015:Methanococcales / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009249:NADP / Q000737:chemistry; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity; D040681:Structural Homology, Protein
chemical_list: D011994:Recombinant Proteins; D009249:NADP; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)