1LNZ

Structure of the Obg GTP-binding protein

Summary for 1LNZ

• Entry DOI: 10.2210/pdb1lnz/pdb
• Descriptor: SPO0B-associated GTP-binding protein, MAGNESIUM ION, GUANOSINE-5',3'-TETRAPHOSPHATE, ... (4 entities in total)
• Functional Keywords: gtpase, obg, stringent factor, stress response, sporulation, large g-protein, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, cell cycle
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 76992.16

Authors

Buglino, J.,Shen, V.,Hakimian, P.,Lima, C.D.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2002-05-04, release date: 2002-09-16, Last modification date: 2024-11-20)

Primary citation

Buglino, J.,Shen, V.,Hakimian, P.,Lima, C.D.
Structural and biochemical analysis of the Obg GTP binding protein
Structure, 10:1581-1592, 2002

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.

PubMed: 12429099
DOI: 10.1016/S0969-2126(02)00882-1

Experimental method

X-RAY DIFFRACTION (2.6 Å)