Signaling by transmembrane proteins shifts gears.
The HAMP domain is present in a large number of transmembrane proteins in prokaryotes including histidine kinases, adenylyl cyclases, chemotaxis receptors, and phosphatases. In this issue of Cell, Hulko et al. (2006) report the NMR structure of a HAMP domain and present data suggesting that it transduces signals through a simple rotation of its four-helix parallel coiled coil.
Inouye
Masayori
M
Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA. inouye@umdnj.edu
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D019611:Archaeoglobus fulgidus / Q000235:genetics / Q000378:metabolism*; D019281:Dimerization; D000071677:Histidine Kinase; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction
D019843:Archaeal Proteins; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; D011494:Protein Kinases; D000071677:Histidine Kinase