Substitution of a Surface-Exposed Residue Involved in an Allosteric Network Enhances Tryptophan Synthase Function in Cells

Substitution of a Surface-Exposed Residue Involved in an Allosteric Network Enhances Tryptophan Synthase Function in Cells

Networks of noncovalent amino acid interactions propagate allosteric signals throughout proteins. Tryptophan synthase (TS) is an allosterically controlled bienzyme in which the indole product of the alpha subunit (αTS) is transferred through a 25 Å hydrophobic tunnel to the active site of the beta s...

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Bibliographic Details
Main Authors: Rebecca N. D’Amico, Yuliana K. Bosken, Kathleen F. O’Rourke, Alec M. Murray, Woudasie Admasu, Chia-en A. Chang, David D. Boehr
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-05-01
Series:Frontiers in Molecular Biosciences
Subjects:
allostery
enzyme regulation
nuclear magnetic resonance
molecular dynamics
TIM barrel
substrate channeling
Online Access:https://www.frontiersin.org/articles/10.3389/fmolb.2021.679915/full

Internet

https://www.frontiersin.org/articles/10.3389/fmolb.2021.679915/full

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