4OXX

Crystal Structure of Cindoxin, Surface Entropy reduction Mutant

4OXX の概要

• エントリーDOI: 10.2210/pdb4oxx/pdb
• 分子名称: Cindoxin, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: flavoprotein, fmn, cindoxin, electron transport
• 由来する生物種: Citrobacter braakii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17327.83

構造登録者

Madrona, Y.,Poulos, T.L. (登録日: 2014-02-07, 公開日: 2014-04-16, 最終更新日: 2023-12-27)

主引用文献

Madrona, Y.,Hollingsworth, S.A.,Tripathi, S.,Fields, J.B.,Rwigema, J.C.,Tobias, D.J.,Poulos, T.L.
Crystal structure of cindoxin, the P450cin redox partner.
Biochemistry, 53:1435-1446, 2014

PubMed Abstract: The crystal structure of the flavin mononucleotide (FMN)-containing redox partner to P450cin, cindoxin (Cdx), has been determined to 1.3 Å resolution. The overall structure is similar to that of the FMN domain of human cytochrome P450 reductase. A Brownian dynamics-molecular dynamics docking method was used to produce a model of Cdx with its redox partner, P450cin. This Cdx-P450cin model highlights the potential importance of Cdx Tyr96 in bridging the FMN and heme cofactors as well P450cin Arg102 and Arg346. Each of the single-site Ala mutants exhibits ~10% of the wild-type activity, thus demonstrating the importance of these residues for binding and/or electron transfer. In the well-studied P450cam system, redox partner binding stabilizes the open low-spin conformation of P450cam and greatly decreases the stability of the oxy complex. In sharp contrast, Cdx does not shift P450cin to a low-spin state, although the stability of oxy-P450cin is decreased 10-fold in the presence of Cdx. This indicates that Cdx may have a modest effect on the open-closed equilibrium in P450cin compared to that in P450cam. It has been postulated that part of the effector role of Pdx on P450cam is to promote a significant structural change that makes available a proton relay network involving Asp251 required for O2 activation. The structure around the corresponding Asp in P450cin, Asp241, provides a possible structural reason for why P450cin is less dependent on its redox partner for functionally important structural changes.

PubMed: 24533927
DOI: 10.1021/bi500010m

実験手法

X-RAY DIFFRACTION (1.21 Å)