title: Signal transduction: Gyrating protein kinases.
abstract: Recently determined structures have linked histidine kinases with class II topoisomerases, the DNA repair enzyme MutL and the molecular chaperone Hsp90. This surprising finding may foreshadow a shift in our understanding of energy coupling mechanisms in signal transduction networks.
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
authors.forename: J
authors.initials: J
authors.lastname: Stock
mesh_terms: D000251:Adenosine Triphosphatases; D001426:Bacterial Proteins / Q000378:metabolism*; D004250:DNA Topoisomerases, Type II / Q000378:metabolism*; D029968:Escherichia coli Proteins; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D000071677:Histidine Kinase; D000070956:MutL Proteins; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D018841:HSP90 Heat-Shock Proteins; C074770:MutL protein, E coli; D011494:Protein Kinases; D000071677:Histidine Kinase; D000251:Adenosine Triphosphatases; D000070956:MutL Proteins; D004250:DNA Topoisomerases, Type II