2A5W

Crystal structure of the oxidized gamma-subunit of the dissimilatory sulfite reductase (DsrC) from Archaeoglobus fulgidus

2A5W の概要

• エントリーDOI: 10.2210/pdb2a5w/pdb
• 関連するPDBエントリー: 1SAU
• 分子名称: sulfite reductase, desulfoviridin-type subunit gamma (dsvC), SULFATE ION (3 entities in total)
• 機能のキーワード: orthogonal helix bundle, oxidoreductase
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 40880.23

構造登録者

Mander, G.J.,Weiss, M.S.,Hedderich, R.,Kahnt, J.,Ermler, U.,Warkentin, E. (登録日: 2005-07-01, 公開日: 2005-09-06, 最終更新日: 2024-11-20)

主引用文献

Mander, G.J.,Weiss, M.S.,Hedderich, R.,Kahnt, J.,Ermler, U.,Warkentin, E.
X-ray structure of the gamma-subunit of a dissimilatory sulfite reductase: Fixed and flexible C-terminal arms.
Febs Lett., 579:4600-4604, 2005

PubMed Abstract: The X-ray structure of the gamma-subunit of the dissimilatory sulfite reductase (DsrC) from Archaeoglobus fulgidus was determined at 1.12 and 2.1A resolution, in the two crystal forms named DsrC(nat) and DsrC(ox) the latter being cocrystallized with the oxidizing agent tert-butyl hydroperoxide. The fold corresponds to that of the homologous protein from Pyrobaculum aerophilum but is significantly more compact. The most interesting, highly conserved C-terminal arm adopts a well-defined conformation in A. fulgidus DsrC in contrast to the completely disordered conformation in P. aerophilum DsrC. The functional relevance of both conformations and of a potentially redox-active disulfide bond between the strictly invariant Cys103 and Cys114 are discussed.

PubMed: 16098517
DOI: 10.1016/j.febslet.2005.07.029

実験手法

X-RAY DIFFRACTION (2.1 Å)