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Title: Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites

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. InYersinia 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 chelatemore » 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.« less

Authors:
ORCiD logo; ORCiD logo; ORCiD logo; ORCiD logo; ; ORCiD logo
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
UNIVERSITY
OSTI Identifier:
1372249
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D. Structural Biology; Journal Volume: 73; Journal Issue: 7
Country of Publication:
United States
Language:
ENGLISH
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Radka, Christopher D., DeLucas, Lawrence J., Wilson, Landon S., Lawrenz, Matthew B., Perry, Robert D., and Aller, Stephen G.. Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites. United States: N. p., 2017. Web. doi:10.1107/S2059798317006349.
Radka, Christopher D., DeLucas, Lawrence J., Wilson, Landon S., Lawrenz, Matthew B., Perry, Robert D., & Aller, Stephen G.. Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites. United States. doi:10.1107/S2059798317006349.
Radka, Christopher D., DeLucas, Lawrence J., Wilson, Landon S., Lawrenz, Matthew B., Perry, Robert D., and Aller, Stephen G.. Fri . "Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites". United States. doi:10.1107/S2059798317006349.
@article{osti_1372249,
title = {Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites},
author = {Radka, Christopher D. and DeLucas, Lawrence J. and Wilson, Landon S. and Lawrenz, Matthew B. and Perry, Robert D. and Aller, Stephen G.},
abstractNote = {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. InYersinia 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.},
doi = {10.1107/S2059798317006349},
journal = {Acta Crystallographica. Section D. Structural Biology},
number = 7,
volume = 73,
place = {United States},
year = {Fri Jun 30 00:00:00 EDT 2017},
month = {Fri Jun 30 00:00:00 EDT 2017}
}