4O5R: Crystal Structure Of Alkylhydroperoxide Reductase Subunit C From E. Coli

Citation:
Abstract
Hydroperoxides are reactive oxygen species (ROS) that are toxic to all cells and must be converted into the corresponding alcohols to alleviate oxidative stress. In Escherichia coli, the enzyme primarily responsible for this reaction is alkylhydroperoxide reductase (AhpR). Here, the crystal structures of both of the subunits of EcAhpR, EcAhpF (57 kDa) and EcAhpC (21 kDa), have been solved. The EcAhpF structures (2.0 and 2.65 A resolution) reveal an open and elongated conformation, while that of EcAhpC (3.3 A resolution) forms a decameric ring. Solution X-ray scattering analysis of EcAhpF unravels the flexibility of its N-terminal domain, and its binding to EcAhpC was demonstrated by isothermal titration calorimetry. These studies suggest a novel overall mechanistic model of AhpR as a hydroperoxide scavenger, in which the dimeric, extended AhpF prefers complex formation with the AhpC ring to accelerate the catalytic activity and thus to increase the chance of rescuing the cell from ROS.
PDB ID: 4O5RDownload
MMDB ID: 124465
PDB Deposition Date: 2013/12/20
Updated in MMDB: 2014/11
Experimental Method:
x-ray diffraction
Resolution: 3.33  Å
Source Organism:
Similar Structures:
Biological Unit for 4O5R: decameric; determined by author and by software (PISA)
Molecular Components in 4O5R
Label Count Molecule
Proteins (10 molecules)
10
Ahpc Component, Subunit of Alkylhydroperoxide Reductase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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