6H5L

Kuenenia stuttgartiensis reducing HAO-like protein complex Kustc0457/Kustc0458

6H5L の概要

• エントリーDOI: 10.2210/pdb6h5l/pdb
• 分子名称: Similar to hydroxylamine oxidoreductase, Conserved hypothetical cytochrome protein, HEME C, ... (4 entities in total)
• 機能のキーワード: reductase, anammox, oxidoreductase
• 由来する生物種: Kuenenia stuttgartiensis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91442.00

構造登録者

Dietl, A.,Maalcke, W.,Barends, T.R.M. (登録日: 2018-07-25, 公開日: 2019-04-10, 最終更新日: 2024-10-23)

主引用文献

Dietl, A.,Maalcke, W.J.,Ferousi, C.,Jetten, M.S.M.,Kartal, B.,Barends, T.R.M.
A 60-heme reductase complex from an anammox bacterium shows an extended electron transfer pathway.
Acta Crystallogr D Struct Biol, 75:333-341, 2019

PubMed Abstract: The hydroxylamine oxidoreductase/hydrazine dehydrogenase (HAO/HDH) protein family constitutes an important group of octaheme cytochromes c (OCCs). The majority of these proteins form homotrimers, with their subunits being covalently attached to each other via a rare cross-link between the catalytic heme moiety and a conserved tyrosine residue in an adjacent subunit. This covalent cross-link has been proposed to modulate the active-site heme towards oxidative catalysis by distorting the heme plane. In this study, the crystal structure of a stable complex of an HAO homologue (KsHAOr) with its diheme cytochrome c redox partner (KsDH) from the anammox bacterium Kuenenia stuttgartiensis was determined. KsHAOr lacks the tyrosine cross-link and is therefore tuned to reductive catalysis. The molecular model of the KsHAOr-KsDH complex at 2.6 Å resolution shows a heterododecameric (αβ) assembly, which was also shown to be the oligomeric state in solution by analytical ultracentrifugation and multi-angle static light scattering. The 60-heme-containing protein complex reveals a unique extended electron transfer pathway and provides deeper insights into catalysis and electron transfer in reductive OCCs.

PubMed: 30950404
DOI: 10.1107/S2059798318017473

実験手法

X-RAY DIFFRACTION (2.6 Å)