1lnz | pdb_00001lnz
Structure of the Obg GTP-binding protein
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Overview
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.
About this Structure
1LNZ is a Single protein structure of sequence from Bacillus subtilis with MG and G4P as ligands. Full crystallographic information is available from OCA.
Reference
Structural and biochemical analysis of the Obg GTP binding protein., Buglino J, Shen V, Hakimian P, Lima CD, Structure. 2002 Nov;10(11):1581-92. PMID:12429099
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Bacillus subtilis
- Single protein
- Buglino, J.
- Burley, S K.
- Hakimian, P.
- Lima, C D.
- NYSGXRC, New York Structural GenomiX Research Consortium.
- Shen, V.
- G4P
- MG
- Gtpase
- Large g-protein
- New york structural genomix research consortium
- Nysgxrc
- Obg
- Protein structure initiative
- Psi
- Sporulation
- Stress response
- Stringent factor
- Structural genomics
