Structural and biochemical analysis of the Obg GTP binding protein

Structure. 2002 Nov;10(11):1581-92. doi: 10.1016/s0969-2126(02)00882-1.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / metabolism
  • Crystallography, X-Ray
  • GTP Phosphohydrolases / metabolism
  • Glycine / chemistry
  • Humans
  • Hydrolysis
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleotides / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid


  • Nucleotides
  • GTP Phosphohydrolases
  • Glycine

Associated data

  • PDB/1NLZ