rdf:type |
|
lifeskim:mentions |
umls-concept:C0678594,
umls-concept:C1514562,
umls-concept:C1551356,
umls-concept:C1553422,
umls-concept:C1705165,
umls-concept:C1706201,
umls-concept:C1709850,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2700061
|
pubmed:issue |
12
|
pubmed:dateCreated |
2000-2-3
|
pubmed:databankReference |
|
pubmed:abstractText |
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:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0969-2126
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
7
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1517-26
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10647182-Amino Acid Sequence,
pubmed-meshheading:10647182-Bacterial Proteins,
pubmed-meshheading:10647182-Binding Sites,
pubmed-meshheading:10647182-Crystallography, X-Ray,
pubmed-meshheading:10647182-Hemeproteins,
pubmed-meshheading:10647182-Magnesium,
pubmed-meshheading:10647182-Molecular Sequence Data,
pubmed-meshheading:10647182-Phosphorylation,
pubmed-meshheading:10647182-Protein Conformation,
pubmed-meshheading:10647182-Protein Folding,
pubmed-meshheading:10647182-Protein Structure, Secondary,
pubmed-meshheading:10647182-Sequence Alignment,
pubmed-meshheading:10647182-Sequence Homology, Amino Acid,
pubmed-meshheading:10647182-Signal Transduction
|
pubmed:year |
1999
|
pubmed:articleTitle |
Structural transitions in the FixJ receiver domain.
|
pubmed:affiliation |
Groupe de Cristallographie Biologique, CNRS-IPBS, Toulouse, France.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|