Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/142463
Title: Atomic structure and enzymatic insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C
Authors: Pan, Ankita
Balakrishna, Asha Manikkoth
Nartey, Wilson
Kohlmeier, Andreas
Dip, Phat Vinh
Bhushan, Shashi
Grüber, Gerhard
Keywords: Science::Biological sciences
Issue Date: 2017
Source: Pan, A., Balakrishna, A. M., Nartey, W., Kohlmeier, A., Dip, P. V., Bhushan, S., & Grüber, G. (2018). Atomic structure and enzymatic insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C. Free Radical Biology and Medicine, 115, 252-265. doi:10.1016/j.freeradbiomed.2017.12.003
Journal: Free Radical Biology and Medicine
Abstract: The Enterococcus faecalis alkyl hydroperoxide reductase complex (AhpR) with its subunits AhpC (EfAhpC) and AhpF (EfAhpF) are of paramount importance to restore redox homeostasis. Recently, the novel phenomenon of swapping of the catalytic domains of EfAhpF was uncovered. Here, we visualized its counterpart EfAhpC (187 residues) from the vancomycin-resistant E. faecalis (V583) bacterium by electron microscopy and demonstrate, that in contrast to other bacterial AhpCs, EfAhpC forms a stable decamer-ring irrespective of the redox state. The first crystallographic structure (2.8Å resolution) of the C-terminal truncated form (EfAhpC1-172) confirms the decamer ring and provides new insight into a transition state in-between a fully folded to a locally unfolded conformation in the catalytic center due to redox modulation. Amino acid substitutions of residues in the N- and C-termini as well as the oligomeric interphase of EfAhpC provide information into their structural and enzymatic roles. Mutagenesis, enzymatic and biophysical studies reveal the effect of the unusual existence of four cysteines in EfAhpC, which might optimize the functional adaptation of the E. faecalis enzyme under various physiological conditions.
URI: https://hdl.handle.net/10356/142463
ISSN: 0891-5849
DOI: 10.1016/j.freeradbiomed.2017.12.003
Rights: © 2017 Elsevier Inc. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
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