2EIX

The Structure of Physarum polycephalum cytochrome b5 reductase

2EIX の概要

• エントリーDOI: 10.2210/pdb2eix/pdb
• 関連するPDBエントリー: 1UMK
• 分子名称: NADH-cytochrome b5 reductase, IODIDE ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: flavoprotein, fad-binding domain, nadh-binding, oxidoreductase
• 由来する生物種: Physarum polycephalum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57875.17

構造登録者

Kim, S.W.,Suga, M.,Ogasahara, K.,Ikegami, T.,Minami, Y.,Yubisui, T.,Tsukihara, T. (登録日: 2007-03-14, 公開日: 2007-04-17, 最終更新日: 2023-10-25)

主引用文献

Kim, S.,Suga, M.,Ogasahara, K.,Ikegami, T.,Minami, Y.,Yubisui, T.,Tsukihara, T.
Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution.
Acta Crystallogr.,Sect.F, 63:274-279, 2007

PubMed Abstract: Physarum polycephalum cytochrome b(5) reductase catalyzes the reduction of cytochrome b(5) by NADH. The structure of P. polycephalum cytochrome b(5) reductase was determined at a resolution of 1.56 A. The molecular structure was compared with that of human cytochrome b(5) reductase, which had previously been determined at 1.75 A resolution [Bando et al. (2004), Acta Cryst. D60, 1929-1934]. The high-resolution structure revealed conformational differences between the two enzymes in the adenosine moiety of the FAD, the lid region and the linker region. The structural properties of both proteins were inspected in terms of hydrogen bonding, ion pairs, accessible surface area and cavity volume. The differences in these structural properties between the two proteins were consistent with estimates of their thermostabilities obtained from differential scanning calorimetry data.

PubMed: 17401193
DOI: 10.1107/S1744309107010731

実験手法

X-RAY DIFFRACTION (1.56 Å)