4mh2

Crystal structure of Bovine Mitochondrial Peroxiredoxin III

spinqualitylabelsall models 4mh2, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mh2 is a 12 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CIT Related: 4mh3, 1zye Gene: AOP1, PRDX3 (BOVIN) Activity: Peroxiredoxin, with EC number 1.11.1.15 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PRDX3_BOVIN] Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Publication Abstract from PubMed Mitochondrial 2-cys peroxiredoxin III (PrxIII) is a key player in antioxidant defence reducing locally-generated H2O2 to H2O. A Phe to Leu (F190L) mutation in the C-terminal alpha-helix of PrxIII, mimicking that found in some bacteria and parasites, increases its resistance to hyperoxidation but has no obvious influence on peroxidase activity. Here we report on the oxidized and reduced crystal structures of bovine PrxIII F190L at 2.4 A and 2.2 A, respectively. Both structures exist as two-ring catenanes with their dodecameric rings inclined at 55o to each other, similar to that previously reported for PrxIII C168S. The new higher-resolution structures reveal details of the complex network of H-bonds stabilising the inter-toroid contacts. In addition, Arg123, the key conserved residue, that normally interacts with the catalytic cys (Cp, cys 47) is found in a distinct conformation extending away from the Cp while the characteristic Arg-Glu-Arg network, underpinning the active-site geometry also displays a distinctive arrangement, not observed previously. This novel active-site organisation may provide new insights into the dynamics of the large-scale conformational changes occurring between oxidized and reduced states. Improved Catenated Structures of Bovine Peroxiredoxin III F190L Reveal Details of Ring-Ring Interactions and a Novel Conformational State.,Cao Z, McGow DP, Shepherd C, Lindsay JG PLoS One. 2015 Apr 23;10(4):e0123303. doi: 10.1371/journal.pone.0123303., eCollection 2015. PMID:25906064 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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