4O5Q

Crystal Structure of the Alkylhydroperoxide Reductase AhpF from Escherichia coli

Summary for 4O5Q

• Entry DOI: 10.2210/pdb4o5q/pdb
• Related: 1FL2 4o5r 4o5u
• Descriptor: Alkyl hydroperoxide reductase subunit F, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (9 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 59771.40

Authors

Dip, P.V.,Kamariah, N.,Manimekalai, M.S.S.,Balakrishna, A.M.,Gruber, G. (deposition date: 2013-12-20, release date: 2014-11-05, Last modification date: 2024-10-30)

Primary citation

Dip, P.V.,Kamariah, N.,Subramanian Manimekalai, M.S.,Nartey, W.,Balakrishna, A.M.,Eisenhaber, F.,Eisenhaber, B.,Gruber, G.
Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli
Acta Crystallogr.,Sect.D, 70:2848-2862, 2014

PubMed 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 Å resolution) reveal an open and elongated conformation, while that of EcAhpC (3.3 Å 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.

PubMed: 25372677
DOI: 10.1107/S1399004714019233

Experimental method

X-RAY DIFFRACTION (2 Å)