Structural highlights
Function
[PRDX3_BOVIN] Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A crystal structure is reported for the C168S mutant of a typical 2-Cys peroxiredoxin III (Prx III) from bovine mitochondria at a resolution of 3.3 A. Prx III is present as a two-ring catenane comprising two interlocking dodecameric toroids that are assembled from basic dimeric units. Each ring has an external diameter of 150 A and encompasses a central cavity that is 70 A in width. The concatenated dodecamers are inclined at an angle of 55 degrees, which provides a large contact surface between the rings. Dimer-dimer contacts involved in toroid formation are hydrophobic in nature, whereas the 12 areas of contact between interlocked rings arise from polar interactions. These two major modes of subunit interaction provide important insights into possible mechanisms of catenane formation.
Bovine mitochondrial peroxiredoxin III forms a two-ring catenane.,Cao Z, Roszak AW, Gourlay LJ, Lindsay JG, Isaacs NW Structure. 2005 Nov;13(11):1661-4. PMID:16271889[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cao Z, Roszak AW, Gourlay LJ, Lindsay JG, Isaacs NW. Bovine mitochondrial peroxiredoxin III forms a two-ring catenane. Structure. 2005 Nov;13(11):1661-4. PMID:16271889 doi:10.1016/j.str.2005.07.021
