2NVE

Soluble domain of Rieske Iron Sulfur Protein

2NVE の概要

• エントリーDOI: 10.2210/pdb2nve/pdb
• 関連するPDBエントリー: 2NVF 2NVG 2NWF 2nuk 2num
• 分子名称: Ubiquinol-cytochrome c reductase iron-sulfur subunit, FE2/S2 (INORGANIC) CLUSTER, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: rieske [2fe-2s] isp, oxidoreductase
• 由来する生物種: Rhodobacter sphaeroides
• 細胞内の位置: Cell membrane; Single-pass membrane protein: Q02762
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15536.17

構造登録者

Kolling, D.K.,Brunzelle, J.S.,Lhee, S.,Crofts, A.R.,Nair, S.K. (登録日: 2006-11-12, 公開日: 2007-02-06, 最終更新日: 2024-10-16)

主引用文献

Kolling, D.J.,Brunzelle, J.S.,Lhee, S.,Crofts, A.R.,Nair, S.K.
Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters.
Structure, 15:29-38, 2007

PubMed Abstract: The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc(1) functions as the initial electron acceptor in the rate-limiting step of the catalytic reaction. Prior studies have established roles for a number of conserved residues that hydrogen bond to ligands of the [2Fe-2S] cluster. We have constructed site-specific variants at two of these residues, measured their thermodynamic and functional properties, and determined atomic resolution X-ray crystal structures for the native protein at 1.2 A resolution and for five variants (Ser-154-->Ala, Ser-154-->Thr, Ser-154-->Cys, Tyr-156-->Phe, and Tyr-156-->Trp) to resolutions between 1.5 A and 1.1 A. These structures and complementary biophysical data provide a molecular framework for understanding the role hydrogen bonds to the cluster play in tuning thermodynamic properties, and hence the rate of this bioenergetic reaction. These studies provide a detailed structure-function dissection of the role of hydrogen bonds in tuning the redox potentials of [2Fe-2S] clusters.

PubMed: 17223530
DOI: 10.1016/j.str.2006.11.012

実験手法

X-RAY DIFFRACTION (1.5 Å)