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Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling

J Mol Biol. 2013-01-01; 
Jennifer M Axe, David D Boehr
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Custom Vector Construction … MtIGPS exists as a monofunctional enzyme. The trpC coding sequence for MtIGPS cloned in pET30a expression vector was purchased from GenScript (New Jersey, USA). The pET30a expression vector was isolated from LOBSTR-BL21 (DE3) host cells using slightly modified … Get A Quote

摘要

The α-subunit of tryptophan synthase (αTS) catalyzes the conversion of indole-3-glycerol phosphate to d-glyceraldehyde-3-phosphate and indole. We propose that allosteric networks intrinsic to αTS are modulated by the binding of the β-subunit to regulate αTS function. Understanding these long-range amino acid networks in αTS thus gives insight into the coordination of the two active sites within TS. In this study, we have used Ala residues as probes for structural and dynamic changes of αTS throughout its catalytic cycle, in the absence of the β-subunit. Projection analysis of the chemical shift changes by site-specific amino acid substitutions and ligand titrations indicates that αTS has three importan... More

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