6ITZ
Peroxiredoxin from Thermococcus kodakaraensis
6ITZ の概要
| エントリーDOI | 10.2210/pdb6itz/pdb |
| 分子名称 | Peroxiredoxin (1 entity in total) |
| 機能のキーワード | hydrogen peroxide, oxidoreductase, dodecamer |
| 由来する生物種 | Thermococcus kodakarensis KOD1 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 49354.73 |
| 構造登録者 | |
| 主引用文献 | Himiyama, T.,Oshima, M.,Uegaki, K.,Nakamura, T. Distinct molecular assembly of homologous peroxiredoxins from Pyrococcus horikoshii and Thermococcus kodakaraensis. J.Biochem., 166:89-95, 2019 Cited by PubMed Abstract: Peroxiredoxins from Pyrococcus horikoshii (PhPrx) and Thermococcus kodakaraensis (TkPrx) are highly homologous proteins sharing 196 of the 216 residues. We previously reported a pentagonal ring-type decameric structure of PhPrx. Here, we present the crystal structure of TkPrx. Despite their homology, unlike PhPrx, the quaternary structure of TkPrx was found to be a dodecamer comprised of six homodimers arranged in a hexagonal ring-type assembly. The possibility of the redox-dependent conversion of the molecular assembly, which had been observed in PhPrx, was excluded for TkPrx based on the crystal structure of a mutant in which all of the cysteine residues were substituted with serine. The monomer structures of the dodecameric TkPrx and decameric PhPrx coincided well, but there was a slight difference in the relative orientation of the two domains. Molecular assembly of PhPrx and TkPrx in solution evaluated by gel-filtration chromatography was consistent with the crystallographic results. For both PhPrx and TkPrx, the gel-filtration elution volume slightly increased with a decrease in the protein concentration, suggesting the existence of an equilibrium state between the decameric/dodecameric ring and lower-order assembly. This structural assembly difference between highly homologous Prxs suggests a significant influence of quaternary structure on function, worthy of further exploration. PubMed: 30796432DOI: 10.1093/jb/mvz013 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.96 Å) |
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