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Science 28 June 1991:
Vol. 252. no. 5014, pp. 1845 - 1848
DOI: 10.1126/science.2063197
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Articles

Science, Vol 252, Issue 5014, 1845-1848
Copyright © 1991 by American Association for the Advancement of Science

articles

Subunit communication in the anthranilate synthase complex from Salmonella typhimurium

MG Caligiuri and R Bauerle

Department of Biology, University of Virginia, Charlottesville 22901.

The anthranilate synthase-phosphoribosyl transferase complex of the tryptophan biosynthetic pathway in Salmonella typhimurium is an allosteric, heterotetrameric (TrpE2-TrpD2) enzyme whose multiple activities are negatively feedback-regulated by L-tryptophan. A hybrid complex containing one catalytically active, feedback-insensitive and one catalytically inactive, feedback-sensitive mutant TrpE subunit was assembled in vitro and used to investigate communication between regulatory and catalytic sites located on different subunits. The properties of the hybrid complex demonstrate that the binding of a single inhibitor molecule to one TrpE subunit is sufficient for the propagation of a conformational change that affects the active site of the companion subunit.


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The crystal structure of anthranilate synthase from Sulfolobus solfataricus: Functional implications.
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DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
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