9ps9 | pdb_00009ps9

High-resolution crystal structure of Vibrio cholerae NFeoB in the apo form in orthorhombic space group

spinqualitylabelsall models 9ps9, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ps9 is a 4 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: ETF, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A655NVH2_VIBCL Probable transporter of a GTP-driven Fe(2+) uptake system.[RuleBase:RU362098] Publication Abstract from PubMed The acquisition of iron is critical for the survival and the virulence of numerous infectious pathogens, and most bacteria acquire ferrous iron (Fe(2+)) 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. The Structure of the Full Catalytic Cycle of Vibrio cholerae NFeoB.,Magante K, Armstrong CM, Lee M, Smith AT J Mol Biol. 2026 May 1;438(9):169727. doi: 10.1016/j.jmb.2026.169727. Epub 2026 , Feb 20. PMID:41724262 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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