title: Structural and biochemical analysis of the Obg GTP binding protein.
abstract: The Obg nucleotide binding protein family has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to man. Members of the family contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain. Structural analysis of Bacillus subtilis Obg revealed respective domain architectures and how they are coupled through the putative switch elements of the C-terminal GTPase domain in apo and nucleotide-bound configurations. Biochemical analysis of bacterial and human Obg proteins combined with the structural observation of the ppGpp nucleotide within the Obg active sight suggest a potential role for ppGpp modulation of Obg function in B. subtilis.
authors.affiliation: Biochemistry Department, Structural Biology Program, Weill Medical College of Cornell University, New York, NY 10021, USA.
authors.forename: John
authors.initials: J
authors.lastname: Buglino
authors.forename: Vincent
authors.initials: V
authors.lastname: Shen
authors.forename: Payam
authors.initials: P
authors.lastname: Hakimian
authors.forename: Christopher D
authors.initials: CD
authors.lastname: Lima
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000378:metabolism; D018360:Crystallography, X-Ray; D020558:GTP Phosphohydrolases / Q000378:metabolism; D005998:Glycine / Q000737:chemistry; D006801:Humans; D006868:Hydrolysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009711:Nucleotides / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
chemical_list: D009711:Nucleotides; D020558:GTP Phosphohydrolases; D005998:Glycine