Affordable Access

A piston model for transmembrane signaling of the aspartate receptor.

Authors
Type
Published Article
Journal
Science
Publisher
American Association for the Advancement of Science (AAAS)
Volume
285
Issue
5434
Pages
1751–1754
Source
UCSC Cancer biomedical-ucsc
License
Unknown

Abstract

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 approximately 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.

Report this publication

Statistics

Seen <100 times