8FXD
Rubrerythrin from B. pseudomallei: manganese-bound
Summary for 8FXD
Entry DOI | 10.2210/pdb8fxd/pdb |
Descriptor | Rubrerythrin, DI(HYDROXYETHYL)ETHER, MANGANESE (II) ION, ... (4 entities in total) |
Functional Keywords | metalloprotein, oxidative stress, non-heme, oxidoreductase |
Biological source | Burkholderia pseudomallei |
Total number of polymer chains | 6 |
Total formula weight | 113334.43 |
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 citation | 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 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: 40501712DOI: 10.1101/2025.06.01.657255 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
Download full validation report
