1D5W

PHOSPHORYLATED FIXJ RECEIVER DOMAIN

Summary for 1D5W

• Entry DOI: 10.2210/pdb1d5w/pdb
• Descriptor: TRANSCRIPTIONAL REGULATORY PROTEIN FIXJ, SULFATE ION (3 entities in total)
• Functional Keywords: doubly wound five-stranded beta/alpha fold, phosphorylated protein, nitrogen fixation regulation, gene regulation
• Biological source: Sinorhizobium meliloti
• Cellular location: Cytoplasm (Probable): P10958
• Total number of polymer chains: 3
• Total formula weight: 42264.21

Authors

Birck, C.,Mourey, L.,Gouet, P.,Fabry, B.,Schumacher, J.,Rousseau, P.,Kahn, D.,Samama, J.P. (deposition date: 1999-10-12, release date: 2000-10-11, Last modification date: 2021-11-03)

Primary citation

Birck, C.,Mourey, L.,Gouet, P.,Fabry, B.,Schumacher, J.,Rousseau, P.,Kahn, D.,Samama, J.P.
Conformational changes induced by phosphorylation of the FixJ receiver domain.
Structure Fold.Des., 7:1505-1515, 1999

PubMed Abstract: A variety of bacterial adaptative cellular responses to environmental stimuli are mediated by two-component signal transduction pathways. In these phosphorelay cascades, histidine kinases transphosphorylate a conserved aspartate in the receiver domain, a conserved module in the response regulator superfamily. The main effect of this phosphorylation is to alter the conformation of the response regulator in order to modulate its biological function. The response regulator FixJ displays a typical modular arrangement, with a phosphorylatable N-terminal receiver domain and a C-terminal DNA-binding domain. In the symbiotic bacterium Sinorhizobium meliloti, phosphorylation of this response regulator activates transcription of nitrogen-fixation genes.

PubMed: 10647181
DOI: 10.1016/S0969-2126(00)88341-0

Experimental method

X-RAY DIFFRACTION (2.3 Å)