Signal transduction at a protein synapse.
Contraction of the bacteriophage T4 tail in the act of host cell penetration represents a massive structural change powered by conformational free energy. A paper in this issue of Cell by compares cryo-electron microscopic reconstructions of the initial and final states and reveals that the basic underlying mechanism is concerted rigid-body movements of the constituent protein subunits, akin to the tumbling of gears in a lock.
Steven
Alasdair C
AC
Laboratory of Structural Biology, NIAMS, Building 50, Room 1517, 50 South Drive MSC 8025, National Institutes of Health, Bethesda, MD 20892, USA.
D020816:Amino Acid Motifs; D017122:Bacteriophage T4 / Q000378:metabolism; D020285:Cryoelectron Microscopy; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*; D015398:Signal Transduction; D013569:Synapses / Q000378:metabolism* / Q000502:physiology; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism
D011506:Proteins; D014764:Viral Proteins