3X33

Crystal structure of the oxidized form of the solubilized domain of porcine cytochrome b5 in form 2 crystal

3X33 の概要

• エントリーDOI: 10.2210/pdb3x33/pdb
• 関連するPDBエントリー: 3X32 3X34 3X35
• 分子名称: Cytochrome b5, PROTOPORPHYRIN IX CONTAINING FE, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: heme, electron transport
• 由来する生物種: Sus scrofa (Pig)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11446.42

構造登録者

Hirano, Y.,Kimura, S.,Tamada, T. (登録日: 2015-01-14, 公開日: 2015-07-15, 最終更新日: 2023-11-08)

主引用文献

Hirano, Y.,Kimura, S.,Tamada, T.
High-resolution crystal structures of the solubilized domain of porcine cytochrome b5.
Acta Crystallogr.,Sect.D, 71:1572-1581, 2015

PubMed Abstract: Mammalian microsomal cytochrome b5 has multiple electron-transfer partners that function in various electron-transfer reactions. Four crystal structures of the solubilized haem-binding domain of cytochrome b5 from porcine liver were determined at sub-angstrom resolution (0.76-0.95 Å) in two crystal forms for both the oxidized and reduced states. The high-resolution structures clearly displayed the electron density of H atoms in some amino-acid residues. Unrestrained refinement of bond lengths revealed that the protonation states of the haem propionate group may be involved in regulation of the haem redox properties. The haem Fe coordination geometry did not show significant differences between the oxidized and reduced structures. However, structural differences between the oxidized and reduced states were observed in the hydrogen-bond network around the axial ligand His68. The hydrogen-bond network could be involved in regulating the redox states of the haem group.

PubMed: 26143928
DOI: 10.1107/S1399004715009438

実験手法

X-RAY DIFFRACTION (0.93 Å)