Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/105780
Title: Effect of A22 on the conformation of bacterial actin MreB
Authors: Awuni, Elvis
Mu, Yuguang
Keywords: Molecular Dynamics
Simulations
DRNTU::Science::Biological sciences
Issue Date: 2019
Source: Awuni, E., & Mu, Y. (2019). Effect of A22 on the conformation of bacterial actin MreB. International Journal of Molecular Sciences, 20(6), 1304-. doi:10.3390/ijms20061304
Series/Report no.: International Journal of Molecular Sciences
Abstract: The mechanism of the antibiotic molecule A22 is yet to be clearly understood. In a previous study, we carried out molecular dynamics simulations of a monomer of the bacterial actin-like MreB in complex with different nucleotides and A22, and suggested that A22 impedes the release of Pi from the active site of MreB after the hydrolysis of ATP, resulting in filament instability. On the basis of the suggestion that Pi release occurs on a similar timescale to polymerization and that polymerization can occur in the absence of nucleotides, we sought in this study to investigate a hypothesis that A22 impedes the conformational change in MreB that is required for polymerization through molecular dynamics simulations of the MreB protofilament in the apo, ATP+, and ATP-A22+ states. We suggest that A22 inhibits MreB in part by antagonizing the ATP-induced structural changes required for polymerization. Our data give further insight into the polymerization/depolymerization dynamics of MreB and the mechanism of A22.
URI: https://hdl.handle.net/10356/105780
http://hdl.handle.net/10220/48773
ISSN: 1661-6596
DOI: 10.3390/ijms20061304
Rights: © 2019 The Authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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