4WZ7

Crystal structure of mitochondrial NADH:ubiquinone oxidoreductase from Yarrowia lipolytica.

これはPDB形式変換不可エントリーです。

4WZ7 の概要

• エントリーDOI: 10.2210/pdb4wz7/pdb
• 分子名称: NADH-ubiquinone oxidoreductase chain 1, 39-kDa subunit, NUGM protein, ... (50 entities in total)
• 機能のキーワード: complex i, respiratory chain, oxidoreductase, mitochondria
• 由来する生物種: Yarrowia lipolytica; 詳細
• 細胞内の位置: Mitochondrion membrane ; Multi- pass membrane protein : Q9B6D4 Q9B6E9
• タンパク質・核酸の鎖数: 67
• 化学式量合計: 656099.59

構造登録者

Wirth, C.,Zickermann, V.,Brandt, U.,Hunte, C. (登録日: 2014-11-18, 公開日: 2015-03-25, 最終更新日: 2024-10-09)

主引用文献

Zickermann, V.,Wirth, C.,Nasiri, H.,Siegmund, K.,Schwalbe, H.,Hunte, C.,Brandt, U.
Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I.
Science, 347:44-49, 2015

PubMed Abstract: Proton-pumping complex I of the mitochondrial respiratory chain is among the largest and most complicated membrane protein complexes. The enzyme contributes substantially to oxidative energy conversion in eukaryotic cells. Its malfunctions are implicated in many hereditary and degenerative disorders. We report the x-ray structure of mitochondrial complex I at a resolution of 3.6 to 3.9 angstroms, describing in detail the central subunits that execute the bioenergetic function. A continuous axis of basic and acidic residues running centrally through the membrane arm connects the ubiquinone reduction site in the hydrophilic arm to four putative proton-pumping units. The binding position for a substrate analogous inhibitor and blockage of the predicted ubiquinone binding site provide a model for the "deactive" form of the enzyme. The proposed transition into the active form is based on a concerted structural rearrangement at the ubiquinone reduction site, providing support for a two-state stabilization-change mechanism of proton pumping.

PubMed: 25554780
DOI: 10.1126/science.1259859

実験手法

X-RAY DIFFRACTION (3.6 Å)