1DBW
CRYSTAL STRUCTURE OF FIXJ-N
Summary for 1DBW
Entry DOI | 10.2210/pdb1dbw/pdb |
Related | 1D5W 1DCK 1DCM |
Descriptor | TRANSCRIPTIONAL REGULATORY PROTEIN FIXJ, POLYETHYLENE GLYCOL (N=34) (3 entities in total) |
Functional Keywords | doubly wound five-stranded beta/alpha fold, nitrogen fixation regulation, transcription |
Biological source | Sinorhizobium meliloti |
Cellular location | Cytoplasm : P10958 |
Total number of polymer chains | 2 |
Total formula weight | 29289.85 |
Authors | Gouet, P.,Fabry, B.,Guillet, V.,Birck, C.,Mourey, L.,Kahn, D.,Samama, J.P. (deposition date: 1999-11-03, release date: 1999-11-26, Last modification date: 2024-02-07) |
Primary citation | Gouet, P.,Fabry, B.,Guillet, V.,Birck, C.,Mourey, L.,Kahn, D.,Samama, J.P. Structural transitions in the FixJ receiver domain. Structure Fold.Des., 7:1517-1526, 1999 Cited by PubMed Abstract: Two-component signal transduction pathways are sophisticated phosphorelay cascades widespread in prokaryotes and also found in fungi, molds and plants. FixL/FixJ is a prototypical system responsible for the regulation of nitrogen fixation in the symbiotic bacterium Sinorhizobium meliloti. In microaerobic conditions the membrane-bound kinase FixL uses ATP to transphosphorylate a histidine residue, and the response regulator FixJ transfers the phosphoryl group from the phosphohistidine to one of its own aspartate residues in a Mg(2+)-dependent mechanism. PubMed: 10647182DOI: 10.1016/S0969-2126(00)88342-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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