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Unveiling the activation dynamics of a fold-switch bacterial glycosyltransferase by F NMR

J Biol Chem. 2020; 
Jobst Liebau, Montse Tersa, Beatriz Trastoy, Joan Patrick, Ane Rodrigo-Unzueta, Francisco Corzana, Tobias Sparrman, Marcelo E Guerin, Lena Mäler
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PCR Cloning and Subcloning … Cloning and purification of wild type PimA and PimA mutants PimAR144C and PimAT126C-V359C-R144C mutants of PimA from Mycobacterium smegmatis, were obtained from GenScript using pET29a-pimA as the DNA template (26) … Get A Quote

摘要

Fold-switch pathways remodel the secondary structure topology of proteins in response to the cellular environment. It is a major challenge to understand the dynamics of these folding processes. Here, we conducted an in-depth analysis of the α-helix-to-β-strand and β-strand-to-α-helix transitions and domain motions displayed by the essential mannosyltransferase PimA from mycobacteria. Using F NMR, we identified four functionally relevant states of PimA that coexist in dynamic equilibria on millisecond-to-second timescales in solution. We discovered that fold-switching is a slow process, on the order of seconds, whereas domain motions occur simultaneously but are substantially faster, on the order of millisec... More

关键词

19F NMR, carbohydrate active enzymes, conformational dynamics, enzyme catalysis, glycosyltransferases, protein fold-switching, protein dynamics, protein function, protein structure, relaxation dispersion