6EFV

The NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation that is unique to this diflavin reductase

6EFV の概要

• エントリーDOI: 10.2210/pdb6efv/pdb
• 分子名称: Sulfite reductase [NADPH] flavoprotein alpha-component, FLAVIN-ADENINE DINUCLEOTIDE, FLAVIN MONONUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: sulfite reductase, sulfite reductase flavoprotein, cytochrome p450 reductase, fad, fmn, electron transfer, flavoprotein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65868.06

構造登録者

Tavolieri, A.M.,Askenasy, I.,Murray, D.T.,Pennington, J.M.,Stroupe, M.E. (登録日: 2018-08-17, 公開日: 2019-02-27, 最終更新日: 2023-10-11)

主引用文献

Tavolieri, A.M.,Murray, D.T.,Askenasy, I.,Pennington, J.M.,McGarry, L.,Stanley, C.B.,Stroupe, M.E.
NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase.
J. Struct. Biol., 205:170-179, 2019

PubMed Abstract: This is the first X-ray crystal structure of the monomeric form of sulfite reductase (SiR) flavoprotein (SiRFP-60) that shows the relationship between its major domains in an extended position not seen before in any homologous diflavin reductases. Small angle neutron scattering confirms this novel domain orientation also occurs in solution. Activity measurements of SiR and SiRFP variants allow us to propose a novel mechanism for electron transfer from the SiRFP reductase subunit to its oxidase metalloenzyme partner that, together, make up the SiR holoenzyme. Specifically, we propose that SiR performs its 6-electron reduction via intramolecular or intermolecular electron transfer. Our model explains both the significance of the stoichiometric mismatch between reductase and oxidase subunits in the holoenzyme and how SiR can handle such a large volume electron reduction reaction that is at the heart of the sulfur bio-geo cycle.

PubMed: 30654136
DOI: 10.1016/j.jsb.2019.01.001

実験手法

X-RAY DIFFRACTION (2.341 Å)