2HLS

The crystal structure of a protein disulfide oxidoreductase from Aeropyrum pernix k1

2HLS の概要

• エントリーDOI: 10.2210/pdb2hls/pdb
• 分子名称: protein disulfide oxidoreductase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: protein disulfide oxidoreductase, thioredoxin fold, oxidoreductase
• 由来する生物種: Aeropyrum pernix
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54799.19

構造登録者

D'Ambrosio, K.,De Simone, G. (登録日: 2006-07-10, 公開日: 2006-10-03, 最終更新日: 2024-10-16)

主引用文献

D'Ambrosio, K.,Pedone, E.,Langella, E.,De Simone, G.,Rossi, M.,Pedone, C.,Bartolucci, S.
A Novel Member of the Protein Disulfide Oxidoreductase Family from Aeropyrum pernix K1: Structure, Function and Electrostatics.
J.Mol.Biol., 362:743-752, 2006

PubMed Abstract: The formation of disulfide bonds between cysteine residues is a rate-limiting step in protein folding. To control this oxidative process, different organisms have developed different systems. In bacteria, disulfide bond formation is assisted by the Dsb protein family; in eukarya, disulfide bond formation and rearrangement are catalyzed by PDI. In thermophilic organisms, a potential key role in disulfide bond formation has recently been ascribed to a new cytosolic Protein Disulphide Oxidoreductase family whose members have a molecular mass of about 26 kDa and are characterized by two thioredoxin folds comprising a CXXC active site motif each. Here we report on the functional and structural characterization of ApPDO, a new member of this family, which was isolated from the archaeon Aeropyrum pernix K1. Functional studies have revealed that ApPDO can catalyze the reduction, oxidation and isomerization of disulfide bridges. Structural studies have shown that this protein has two CXXC active sites with fairly similar geometrical parameters typical of a stable conformation. Finally, a theoretical calculation of the cysteine pK(a) values has suggested that the two active sites have similar functional properties and each of them can impart activity to the enzyme. Our results are evidence of functional similarity between the members of the Protein Disulphide Oxidoreductase family and the eukaryotic enzyme PDI. However, as the different three-dimensional features of these two biological systems strongly suggest significantly different mechanisms of action, further experimental studies will be needed to make clear how different three-dimensional structures can result in systems with similar functional behavior.

PubMed: 16934838
DOI: 10.1016/j.jmb.2006.07.038

実験手法

X-RAY DIFFRACTION (1.93 Å)