This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1zye
From Proteopedia
Crystal strucutre analysis of Bovine Mitochondrial Peroxiredoxin III
Overview
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.
About this Structure
1ZYE is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 18:14:05 2008
