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5UYC

YfeA from M9 minimal media supplemented with manganese - Mn wavelength

Summary for 5UYC
Entry DOI10.2210/pdb5uyc/pdb
Related5UXS 5UXU 5UY0 5UY4 5UY5 5UYA 5UYB 5UYD 5UYE 5UYF 5UYG 5UYH
DescriptorPeriplasmic chelated iron-binding protein YfeA, MANGANESE (II) ION (3 entities in total)
Functional Keywordspolyspecific, transition metal, transport, metal transport
Biological sourceYersinia pestis
Cellular locationPeriplasm: Q56952
Total number of polymer chains1
Total formula weight36103.75
Authors
Radka, C.D.,DeLucas, L.J.,Aller, S.G. (deposition date: 2017-02-23, release date: 2017-07-12, Last modification date: 2023-10-04)
Primary citationRadka, C.D.,DeLucas, L.J.,Wilson, L.S.,Lawrenz, M.B.,Perry, R.D.,Aller, S.G.
Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites.
Acta Crystallogr D Struct Biol, 73:557-572, 2017
Cited by
PubMed Abstract: Gram-negative bacteria use siderophores, outer membrane receptors, inner membrane transporters and substrate-binding proteins (SBPs) to transport transition metals through the periplasm. The SBPs share a similar protein fold that has undergone significant structural evolution to communicate with a variety of differentially regulated transporters in the cell. In Yersinia pestis, the causative agent of plague, YfeA (YPO2439, y1897), an SBP, is important for full virulence during mammalian infection. To better understand the role of YfeA in infection, crystal structures were determined under several environmental conditions with respect to transition-metal levels. Energy-dispersive X-ray spectroscopy and anomalous X-ray scattering data show that YfeA is polyspecific and can alter its substrate specificity. In minimal-media experiments, YfeA crystals grown after iron supplementation showed a threefold increase in iron fluorescence emission over the iron fluorescence emission from YfeA crystals grown from nutrient-rich conditions, and YfeA crystals grown after manganese supplementation during overexpression showed a fivefold increase in manganese fluorescence emission over the manganese fluorescence emission from YfeA crystals grown from nutrient-rich conditions. In all experiments, the YfeA crystals produced the strongest fluorescence emission from zinc and could not be manipulated otherwise. Additionally, this report documents the discovery of a novel surface metal-binding site that prefers to chelate zinc but can also bind manganese. Flexibility across YfeA crystal forms in three loops and a helix near the buried metal-binding site suggest that a structural rearrangement is required for metal loading and unloading.
PubMed: 28695856
DOI: 10.1107/S2059798317006349
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.959 Å)
Structure validation

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