Download MendeleyStructural and biochemical analysis of the Obg GTP binding protein
Buglino, J., Shen, V., Hakimian, P., Lima, C.D.(2002) Structure 10: 1581-1592
- PubMed: 12429099
- DOI: https://doi.org/10.1016/s0969-2126(02)00882-1
- Primary Citation of Related Structures:
1LNZ - PubMed 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.
Organizational Affiliation:
Biochemistry Department, Structural Biology Program, Weill Medical College of Cornell University, New York, NY 10021, USA.
