1F04

SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C

1F04 の概要

• エントリーDOI: 10.2210/pdb1f04/pdb
• 関連するPDBエントリー: 1F03
• 分子名称: CYTOCHROME B5, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• 機能のキーワード: cytochrome b5, protein recognition, solution structure, paramagnetic nmr, electron transport
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side: P00171
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9873.75

構造登録者

Wu, Y.B.,Lu, J.,Qian, C.M.,Tang, W.X.,Li, E.C.,Wang, J.F.,Wang, Y.H.,Wang, W.H.,Lu, J.X.,Xie, Y.,Huang, Z.X. (登録日: 2000-05-14, 公開日: 2000-06-21, 最終更新日: 2024-05-22)

主引用文献

Wu, Y.,Wang, Y.,Qian, C.,Lu, J.,Li, E.,Wang, W.,Lu, J.,Xie, Y.,Wang, J.,Zhu, D.,Huang, Z.,Tang, W.
Solution structure of cytochrome b(5) mutant (E44/48/56A/D60A) and its interaction with cytochrome c.
Eur.J.Biochem., 268:1620-1630, 2001

PubMed Abstract: Using 1617 meaningful NOEs with 188 pseudocontact shifts, a family of 35 conformers of oxidized bovine microsomal cytochrome b5 mutant (E44/48/56A/D60A) has been obtained and is characterized by good resolution (rmsd to the mean structure are 0.047 +/- 0.007 nm and 0.095 +/- 0.008 nm for backbone and heavy atoms, respectively). The solution structure of the mutant, when compared with the X-ray structure of wild-type cytochrome b(5), has no significant changes in the whole folding and secondary structure. The binding between cytochrome b(5) and cytochrome c shows that the association constant of the mutant-cytochrome c complex is much lower than the one for wild-type complex (2.2 x 10(4) M(-1) vs. 5.1 x 10(3) M(-1)). The result suggests the four acidic residues have substantial effects on the formation of the complex between cytochrome b(5) and cytochrome c, and therefore it is concluded reasonably that the electrostatic interaction plays an important role in maintaining the stability and specificity of the complex formed. The competition between the ferricytochrome b(5) mutant and [Cr(oxalate)(3)](3-) for ferricytochrome c shows that site III of cytochrome c, which is a strong binding site to wild-type cytochrome b(5), still binds to the mutant with relatively weaker strength. Our results indicate that certain bonding geometries do occur in the interaction between the present mutant and cytochrome c and these geometries, which should be quite different from the ones of the Salemme and Northrup models.

PubMed: 11248680
DOI: 10.1046/j.1432-1327.2001.02033.x

実験手法

SOLUTION NMR