Structural and biochemical analysis of the Obg GTP binding protein.
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.
Buglino
John
J
Biochemistry Department, Structural Biology Program, Weill Medical College of Cornell University, New York, NY 10021, USA.
Shen
Vincent
V
Hakimian
Payam
P
Lima
Christopher D
CD
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
D009711:Nucleotides; D020558:GTP Phosphohydrolases; D005998:Glycine