|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
47
|
|
pubmed:dateCreated |
2009-11-25
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Heme nitric oxide/oxygen (H-NOX) proteins are found in eukaryotes where they are typically part of a larger protein such as soluble guanylate cyclase and in prokaryotes where they are often found in operons with a histidine kinase, suggesting that H-NOX proteins serve as sensors for NO and O(2) in signaling pathways. The Fe(II)-NO complex of the H-NOX protein from Shewanella oneidensis inhibits the autophosphorylation of the operon-associated histidine kinase, whereas the ligand-free H-NOX has no effect on the kinase. NMR spectroscopy was used to determine the structures of the Fe(II)-CO complex of the S. oneidensis H-NOX and the Fe(II)-CO complex of the H103G H-NOX mutant as a mimic of the ligand-free and kinase-inhibitory Fe(II)-NO H-NOX, respectively. The results provide a molecular glimpse into the ligand-induced conformational changes that may underlie kinase inhibition and the subsequent control of downstream signaling.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-11075388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-11142512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-11282350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-11563911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-12590654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-12669648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-15220933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-15287748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-15326296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-15472039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-16094696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-16125437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-16407994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-16728401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-17015012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-17054345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-17215864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-17988156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-18044974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-18556554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-19032091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-19089323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-282600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-6509031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-7503421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-7568117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-7910035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-7966330,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-8230194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-9353189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-9489922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-9521770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-9533688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-9846877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19918063-993515
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
1091-6490
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
24
|
|
pubmed:volume |
106
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
19753-60
|
|
pubmed:dateRevised |
2010-9-27
|
|
pubmed:meshHeading |
pubmed-meshheading:19918063-Animals,
pubmed-meshheading:19918063-Carbon Monoxide,
pubmed-meshheading:19918063-Heme,
pubmed-meshheading:19918063-Molecular Structure,
pubmed-meshheading:19918063-Nitric Oxide,
pubmed-meshheading:19918063-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:19918063-Phosphorylation,
pubmed-meshheading:19918063-Protein Conformation,
pubmed-meshheading:19918063-Protein Kinases,
pubmed-meshheading:19918063-Shewanella,
pubmed-meshheading:19918063-Signal Transduction
|
|
pubmed:year |
2009
|
|
pubmed:articleTitle |
A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation.
|
|
pubmed:affiliation |
Department of Chemistry, University of California, Berkeley, CA 94720-3220, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
|
