5Y63

Crystal structure of Enterococcus faecalis AhpC

5Y63 の概要

• エントリーDOI: 10.2210/pdb5y63/pdb
• 関連するPDBエントリー: 4O5R
• 分子名称: Alkyl hydroperoxide reductase, C subunit (2 entities in total)
• 機能のキーワード: oxidoreductase, 2cys peroxiredoxins
• 由来する生物種: Enterococcus faecalis (strain ATCC 700802 / V583)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 104872.28

構造登録者

Pan, A.,Balakrishna, A.M.,Grueber, G. (登録日: 2017-08-10, 公開日: 2017-12-27, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.87 Å)