1tp9
From Proteopedia
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PRX D (type II) from Populus tremula
Overview
Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce, hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly, conserved cysteine. Very abundant in all organisms, Prxs are produced as, diverse isoforms characterized by different catalytic mechanisms and, various thiol-containing reducing agents. The oligomeric state of Prxs and, the link with their functionality is a subject of intensive research. We, present here a combined X-ray and nuclear magnetic resonance (NMR) study, of a plant Prx that belongs to the D-Prx (type II) subfamily. The Populus, trichocarpa Prx is the first Prx shown to be regenerated in vitro by both, the glutaredoxin and thioredoxin systems. The crystal structure and, solution NMR provide evidence that the reduced protein is a specific, noncovalent homodimer both in the crystal and in solution. The dimer, interface is roughly perpendicular to the plane of the central beta sheet, and differs from the interface of A- and B-Prx dimers, where proteins, associate in the plane parallel to the beta sheet. The homodimer interface, involves residues strongly conserved in the D (type II) Prxs, suggesting, that all Prxs of this family can homodimerize. The study provides a new, insight into the Prx oligomerism and the basis for protein-protein and, enzyme-substrate interaction studies by NMR.
About this Structure
1TP9 is a Single protein structure of sequence from Populus trichocarpa with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism., Echalier A, Trivelli X, Corbier C, Rouhier N, Walker O, Tsan P, Jacquot JP, Aubry A, Krimm I, Lancelin JM, Biochemistry. 2005 Feb 15;44(6):1755-67. PMID:15697201
Page seeded by OCA on Sun Nov 25 02:31:26 2007
