4o5q

Crystal Structure of the Alkylhydroperoxide Reductase AhpF from Escherichia coli

spinqualitylabelsall models 4o5q, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4o5q is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD, FAD, GOL, PG4, PGE, SO4, TRS Related: 1fl2, 4o5u, 4o5r Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AHPF_ECOLI] Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein. Publication Abstract from PubMed 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. Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli.,Dip PV, Kamariah N, Subramanian Manimekalai MS, Nartey W, Balakrishna AM, Eisenhaber F, Eisenhaber B, Gruber G Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):2848-62. doi:, 10.1107/S1399004714019233. Epub 2014 Oct 16. PMID:25372677 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioredoxin Reductase

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