5Y63

Crystal structure of Enterococcus faecalis AhpC

Summary for 5Y63

• Entry DOI: 10.2210/pdb5y63/pdb
• Related: 4O5R
• Descriptor: Alkyl hydroperoxide reductase, C subunit (2 entities in total)
• Functional Keywords: oxidoreductase, 2cys peroxiredoxins
• Biological source: Enterococcus faecalis (strain ATCC 700802 / V583)
• Total number of polymer chains: 5
• Total formula weight: 104872.28

Authors

Pan, A.,Balakrishna, A.M.,Grueber, G. (deposition date: 2017-08-10, release date: 2017-12-27, Last modification date: 2024-10-23)

Primary citation

Pan, A.,Balakrishna, A.M.,Nartey, W.,Kohlmeier, A.,Dip, P.V.,Bhushan, S.,Gruber, G.
Atomic structure and enzymatic insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C
Free Radic. Biol. Med., 115:252-265, 2017

PubMed 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 (EfAhpC) 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.

PubMed: 29223533
DOI: 10.1016/j.freeradbiomed.2017.12.003

Experimental method

X-RAY DIFFRACTION (2.87 Å)