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Science 25 September 1987:
Vol. 237. no. 4822, pp. 1596 - 1600
DOI: 10.1126/science.2820061
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Articles

Science, Vol 237, Issue 4822, 1596-1600
Copyright © 1987 by American Association for the Advancement of Science

articles

Global flexibility in a sensory receptor: a site-directed cross-linking approach

JJ Falke and DE Koshland Jr

The aspartate receptor of Escherichia coli and Salmonella typhimurium is a cell surface sensory transducer that binds extracellular aspartate and sends a transmembrane signal to the inside of the bacterium. The flexibility and allostery of this receptor was examined by placing sulfhydryl groups as potential cross-linking sites at targeted locations in the protein. Seven different mutant receptors were constructed, each containing a single cysteine residue at a different position in the primary structure. Intramolecular disulfide bond formation within oligomers of these mutant receptors is shown to trap structural fluctuations and to detect ligand-induced changes in structure. The results indicate that the receptor oligomer has a flexible, dynamic structure which undergoes a global change upon aspartate binding.


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