Structural and biochemical analysis of the Obg GTP binding protein.
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Buglino J, Shen V, Hakimian P, Lima CD
Structural and biochemical analysis of the Obg GTP binding protein.
Structure. 2002 Nov;10(11):1581-92.
- PubMed ID
- 12429099 [ View in 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.