A Single Mutation Traps a Half-Sites Reactive Enzyme in Mid-Stream, Explaining Asymmetry in Hydride Transfer

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Date: May 15, 2018
From: Biochemistry(Vol. 57, Issue 19)
Publisher: American Chemical Society
Document Type: Report
Length: 66 words

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Abstract :

The study reports 2.4 A X-ray structure of the C-terminal deletion mutant of E. coli TS in complex with a substrate and a cofactor analogue, CB3717.Structure further shows how the binding of the cofactor at one site triggers hydride transfer and borrows needed stabilization from substrate binding at the second site. It indicates pathways through the dimer interface that contribute to allostery relevant to half-sites reactivity.

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Gale Document Number: GALE|A542091440