Probing the Structure of the Escherichia coli Periplasmic Proteins HdeA and YmgD by Molecular Dynamics Simulations

Socher E, Sticht H (2016)


Publication Type: Journal article

Publication year: 2016

Journal

Book Volume: 120

Pages Range: 11845-11855

Journal Issue: 46

DOI: 10.1021/acs.jpcb.6b06091

Abstract

HdeA and YmgD are structurally homologous proteins in the periplasm of Escherichia coli. HdeA has been shown to represent an acid-activated chaperone, whereas the function of YmgD has not yet been characterized. We performed pH-titrating molecular dynamics simulations (pHtMD) to investigate the structural changes of both proteins and to assess whether YmgD may also exhibit an unfolding behavior similar to that of HdeA. The unfolding pathway of HdeA includes partially unfolded dimer structures, which represent a prerequisite for subsequent dissociation. In contrast to the coupled unfolding and dissociation of HdeA, YmgD displays dissociation of the folded subunits, and the subunits do not undergo significant unfolding even at low pH values. The differences in subunit stability between HdeA and YmgD may be explained by the structural features of helix D, which represents the starting point of unfolding in HdeA. In summary, the present study suggests that YmgD either is not an acid-activated chaperone or, at least, does not require unfolding for activation.

Authors with CRIS profile

How to cite

APA:

Socher, E., & Sticht, H. (2016). Probing the Structure of the Escherichia coli Periplasmic Proteins HdeA and YmgD by Molecular Dynamics Simulations. Journal of Physical Chemistry B, 120(46), 11845-11855. https://dx.doi.org/10.1021/acs.jpcb.6b06091

MLA:

Socher, Eileen, and Heinrich Sticht. "Probing the Structure of the Escherichia coli Periplasmic Proteins HdeA and YmgD by Molecular Dynamics Simulations." Journal of Physical Chemistry B 120.46 (2016): 11845-11855.

BibTeX: Download