A single amino acid switch within the "hinge" region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product.

Abstract excerpt

The trpB8 mutation of Escherichia coli causes a major conformational change within the beta subunit of tryptophan synthase. The basis of this effect is a replacement of glycine 281 by arginine within a structurally important "hinge" region. The mutant subunit, beta(B8), is catalytically active only under certain conditions, both in vivo and in vitro. Physiologically, the availability of wild type alpha subunit is...

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