A Piston Model for Transmembrane Signaling of the Aspartate Receptor

Science  10 Sep 1999:
Vol. 285, Issue 5434, pp. 1751-1754
DOI: 10.1126/science.285.5434.1751

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To characterize the mechanism by which receptors propagate conformational changes across membranes, nitroxide spin labels were attached at strategic positions in the bacterial aspartate receptor. By collecting the electron paramagnetic resonance spectra of these labeled receptors in the presence and absence of the ligand aspartate, ligand binding was shown to generate an ∼1 angstrom intrasubunit piston-type movement of one transmembrane helix downward relative to the other transmembrane helix. The receptor-associated phosphorylation cascade proteins CheA and CheW did not alter the ligand-induced movement. Because the piston movement is very small, the ability of receptors to produce large outcomes in response to stimuli is caused by the ability of the receptor-coupled enzymes to detect small changes in the conformation of the receptor.

  • * These authors contributed equally to this work.

  • Present address: Departments of Biology and Environmental Toxicology, University of California at Santa Cruz, CA 95064, USA.

  • To whom correspondence should be addressed. E-mail: shin{at} (Y.-K.S.); dek{at} (D.E.K).

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