9ONN

Co-bound B. pseudomallei Rubrerythrin

9ONN の概要

• エントリーDOI: 10.2210/pdb9onn/pdb
• 関連するPDBエントリー: 8FUH 8FVV 8FXD 9ONM 9ONO 9ONQ 9ONR
• 分子名称: Rubrerythrin, COBALT (II) ION (3 entities in total)
• 機能のキーワード: peroxidase, metal binding protein
• 由来する生物種: Burkholderia pseudomallei
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 93190.24

構造登録者

Budziszewski, G.R.,Snell, M.E.,Monteiro, D.C.F.,Lynch, M.L.,Bowman, S.E.J. (登録日: 2025-05-15, 公開日: 2025-06-25)

主引用文献

Budziszewski, G.R.,Lynch, M.L.,Snell, M.E.,Monteiro, D.C.,Bowman, S.E.
Burkholderia pseudomallei rubrerythrin promiscuously binds metals in a structurally pre-formed bimetallic binding site.
Biorxiv, 2025

PubMed Abstract: Rubrerythrins are a group of proteins within the Ferritin-like superfamily that display a defining four-helix bundle domain. They also show multiple structural features that are crucial to their functionality as iron storage proteins and in detoxification and oxidative stress response. Here we investigate rubrerythrin (Rbr) in multiple metalated states, from the pathogen (). We use X-ray crystallography for structure determination of Rbr to probe the capacity and specificity of metal binding. Rbr lacks the rubredoxin moiety found in canonical Rbrs from anaerobic lineages, and we demonstrate that Rbr also possesses a domain-swapped dimer, which has functional implications for its putative role in oxidative stress response. We also carry out spectroscopic assessment of Rbr with various metals, using energy dispersive X-ray (EDX) spectroscopy. We observe that samples can contain metals other than those supplied in crystallization conditions, and developed a strategy of utilizing EDX spectroscopy to select those samples with single metal incorporation for downstream diffraction data collection. Our work underscores the importance of spectroscopic probing for definitive metal identification and characterization.

PubMed: 40501712
DOI: 10.1101/2025.06.01.657255

実験手法

X-RAY DIFFRACTION (1.53 Å)