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9PSD

High-resolution crystal structure of Vibrio cholerae NFeoB bound to GDP-AlF3

Summary for 9PSD
Entry DOI10.2210/pdb9psd/pdb
DescriptorFerrous iron transport protein B, GLYCEROL, GUANOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
Functional Keywordsfeo, iron, membrane protein, transporter, gtpase, ntpase, metal transport
Biological sourceVibrio cholerae
Total number of polymer chains4
Total formula weight119580.03
Authors
Magante, K.,Lee, M.,Smith, A.T. (deposition date: 2025-07-25, release date: 2026-06-03)
Primary citationMagante, K.,Armstrong, C.M.,Lee, M.,Smith, A.T.
The Structure of the Full Catalytic Cycle of Vibrio cholerae NFeoB.
J.Mol.Biol., 438:169727-169727, 2026
Cited by
PubMed Abstract: The acquisition of iron is critical for the survival and the virulence of numerous infectious pathogens, and most bacteria acquire ferrous iron (Fe) by utilizing the ferrous iron transport (Feo) system. FeoB is the main component of this system and its function is regulated by its soluble cytosolic domain, termed NFeoB. We have recently begun to define the structure and the mechanism of the Feo system from the bacterium Vibrio cholerae, the causative agent of the disease cholera. However, major structural gaps in our understanding of the nucleotide-promiscuous V. cholerae NFeoB still exist. In this work, we have determined several new X-ray crystal structures that reveal distinct snapshots of the VcNFeoB domain in uncommon and unprecedented states, ultimately illuminating the full catalytic cycle of this NTPase. This work reveals important functional features of VcNFeoB that may be leveraged and ultimately targeted to prevent the infectivity and the spread of cholera.
PubMed: 41724262
DOI: 10.1016/j.jmb.2026.169727
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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