1DCK

STRUCTURE OF UNPHOSPHORYLATED FIXJ-N COMPLEXED WITH MN2+

Summary for 1DCK

• Entry DOI: 10.2210/pdb1dck/pdb
• Related: 1D5W 1DBW 1DCM
• Descriptor: TRANSCRIPTIONAL REGULATORY PROTEIN FIXJ, MANGANESE (II) ION, POLYETHYLENE GLYCOL (N=34), ... (4 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: 29454.66

Authors

Gouet, P.,Fabry, B.,Guillet, V.,Birck, C.,Mourey, L.,Kahn, D.,Samama, J.P. (deposition date: 1999-11-05, 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

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: 10647182
DOI: 10.1016/S0969-2126(00)88342-2

Experimental method

X-RAY DIFFRACTION (2 Å)