title: Residue 134 determines the dimer-tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacteria.
abstract: Halomonas nucleoside diphosphate kinase (HaNDK) forms a dimeric assembly and Pseudomonas NDK (PaNDK) forms a tetrameric assembly. The mutation of Glu134 to Ala in HaNDK resulted in the conversion of the native dimeric structure to the tetramer assembly. Conversely, the mutation of Ala134 to Glu in PaNDK lead to the conversion from the tetramer to the dimer assembly, indicating that a single amino acid substitution at position 134 results in an alteration of the oligomeric structure of NDK. By modeling the structure of HaNDK and PaNDK based on the crystal structure of Myxococcus NDK, we showed that Glu134 exerts sufficient repulsive forces to disrupt the dimer-dimer interaction and prevent the formation of the tetramer.
authors.affiliation: Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan. tokunaga@chem.agri.kagoshima-u.ac.jp
authors.forename: Hiroko
authors.initials: H
authors.lastname: Tokunaga
authors.forename: Matsujiro
authors.initials: M
authors.lastname: Ishibashi
authors.forename: Fumio
authors.initials: F
authors.lastname: Arisaka
authors.forename: Shigeki
authors.initials: S
authors.lastname: Arai
authors.forename: Ryota
authors.initials: R
authors.lastname: Kuroki
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Arakawa
authors.forename: Masao
authors.initials: M
authors.lastname: Tokunaga
mesh_terms: D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D019281:Dimerization; D020632:Halomonas / Q000201:enzymology; D008958:Models, Molecular; D009701:Nucleoside-Diphosphate Kinase / Q000737:chemistry* / Q000235:genetics; D021122:Protein Subunits / Q000737:chemistry; D011549:Pseudomonas / Q000201:enzymology
chemical_list: D001426:Bacterial Proteins; D021122:Protein Subunits; D009701:Nucleoside-Diphosphate Kinase