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8FXD

Rubrerythrin from B. pseudomallei: manganese-bound

Summary for 8FXD
Entry DOI10.2210/pdb8fxd/pdb
DescriptorRubrerythrin, DI(HYDROXYETHYL)ETHER, MANGANESE (II) ION, ... (4 entities in total)
Functional Keywordsmetalloprotein, oxidative stress, non-heme, oxidoreductase
Biological sourceBurkholderia pseudomallei
Total number of polymer chains6
Total formula weight113334.43
Authors
Monteiro, D.C.F.,Snell, M.E.,Budziszewski, G.R.,Bowman, S.E.J. (deposition date: 2023-01-24, release date: 2024-02-07, Last modification date: 2025-06-25)
Primary citationBudziszewski, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.58 Å)
Structure validation

239149

數據於2025-07-23公開中

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