2K8V

Solution structure of Oxidised ERp18

2K8V の概要

• エントリーDOI: 10.2210/pdb2k8v/pdb
• NMR情報: BMRB: 7430,15964
• 分子名称: Thioredoxin domain-containing protein 12 (1 entity in total)
• 機能のキーワード: endoplasmic reticulum, thioredoxin fold, oxidase, oxidoreductase, redox-active center
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum lumen: O95881
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17800.96

構造登録者

Rowe, M.L.,Alanen, H.I.,Ruddock, L.W.,Kelly, G.,Schmidt, J.M.,Williamson, R.A.,Howard, M.J. (登録日: 2008-09-25, 公開日: 2009-06-02, 最終更新日: 2024-10-09)

主引用文献

Rowe, M.L.,Ruddock, L.W.,Kelly, G.,Schmidt, J.M.,Williamson, R.A.,Howard, M.J.
Solution structure and dynamics of ERp18, a small endoplasmic reticulum resident oxidoreductase .
Biochemistry, 48:4596-4606, 2009

PubMed Abstract: Here we report the solution structure of oxidized ERp18 as determined using NMR spectroscopy. ERp18 is the smallest member of the protein disulfide isomerase (PDI) family of proteins to contain a Cys-Xxx-Xxx-Cys active site motif. It is an 18 kDa endoplasmic reticulum resident protein with unknown function although sequence similarity to individual domains of the thiol-disulfide oxidoreductase PDI suggests ERp18 may have a similar structure and function. Like the catalytic domains of PDI, ERp18 adopts a thioredoxin fold with a thioredoxin-like active site located at the N-terminus of a long kinked helix that spans the length of the protein. Comparison of backbone chemical shifts for oxidized and reduced ERp18 shows the majority of residues possess the same backbone conformation in both states, with differences limited to the active site and regions in close proximity. S(2) order parameters from NMR backbone dynamics were found to be 0.81 for oxidized and 0.91 for reduced ERp18, and these observations, in combination with amide hydrogen exchange rates, imply a more rigid and compact backbone for the reduced structure. These observations support a putative role for ERp18 within the cell as an oxidase, introducing disulfide bonds to substrate proteins, providing structural confirmation of ERp18's role as a thiol-disulfide oxidoreductase.

PubMed: 19361226
DOI: 10.1021/bi9003342

実験手法

SOLUTION NMR