Issue 26, 2019, Issue in Progress

Single-molecule study on conformational dynamics of M.HhaI

Abstract

We found that apo DNA methyltransferase M.HhaI under the physiological salt concentration does not possess the structure characterized by X-ray crystallography; instead, it interchanges between prefolded and unfolded states. Only after binding to the substrate, it transforms into a crystal-structure-like state. Flipping rates of its catalytic loop were directly measured.

Graphical abstract: Single-molecule study on conformational dynamics of M.HhaI

Supplementary files

Article information

Article type
Paper
Submitted
02 Jan 2019
Accepted
26 Apr 2019
First published
13 May 2019
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2019,9, 14745-14749

Single-molecule study on conformational dynamics of M.HhaI

S. He, C. Yang, S. Peng, C. Chen and X. S. Zhao, RSC Adv., 2019, 9, 14745 DOI: 10.1039/C9RA00021F

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