1V58

Crystal Structure Of the Reduced Protein Disulfide Bond Isomerase DsbG

1V58 の概要

• エントリーDOI: 10.2210/pdb1v58/pdb
• 関連するPDBエントリー: 1V57
• 分子名称: Thiol:disulfide interchange protein dsbG, SULFATE ION (3 entities in total)
• 機能のキーワード: reduced dsbg, redox protein, protein disulfide isomerase, thioredoxin fold, isomerase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P77202
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54480.24

構造登録者

Heras, B.,Edeling, M.A.,Schirra, H.J.,Raina, S.,Martin, J.L. (登録日: 2003-11-21, 公開日: 2004-06-29, 最終更新日: 2024-11-20)

主引用文献

Heras, B.,Edeling, M.A.,Schirra, H.J.,Raina, S.,Martin, J.L.
Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide
Proc.Natl.Acad.Sci.USA, 101:8876-8881, 2004

PubMed Abstract: Dsb proteins control the formation and rearrangement of disulfide bonds during the folding of secreted and membrane proteins in bacteria. DsbG, a member of this family, has disulfide bond isomerase and chaperone activity. Here, we present two crystal structures of DsbG at 1.7and 2.0-A resolution that are meant to represent the reduced and oxidized forms, respectively. The oxidized structure, however, reveals a mixture of both redox forms, suggesting that oxidized DsbG is less stable than the reduced form. This trait would contribute to DsbG isomerase activity, which requires that the active-site Cys residues are kept reduced, regardless of the highly oxidative environment of the periplasm. We propose that a Thr residue that is conserved in the cis-Pro loop of DsbG and DsbC but not found in other Dsb proteins could play a role in this process. Also, the structure of DsbG reveals an unanticipated and surprising feature that may help define its specific role in oxidative protein folding. Thus, the dimensions and surface features of DsbG show a very large and charged binding surface that is consistent with interaction with globular protein substrates having charged surfaces. This finding suggests that, rather than catalyzing disulfide rearrangement in unfolded substrates, DsbG may preferentially act later in the folding process to catalyze disulfide rearrangement in folded or partially folded proteins.

PubMed: 15184683
DOI: 10.1073/pnas.0402769101

実験手法

X-RAY DIFFRACTION (1.7 Å)