Crystal structure of<i>Yersinia pestis</i>virulence factor YfeA reveals two polyspecific metal-binding sites

Radka, C.D.; DeLucas, Lawrence J.; Wilson, Landon; Lawrenz, Matthew B.; Perry, Robert D.; Aller, Stephen G.

doi:10.1107/s2059798317006349

Cited by 17 publications

(40 citation statements)

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“…6). [18] and its related ZnuA from E.coli [20] or MtsA from S. pyogenes [21], FpvC does not possess other metal-binding sites. No interaction could be measured between FpvC and PVD or PVD-Fe 3+ compounds, confirming that FpvC is unable to bind this siderophore [13].…”

Section: Fpvc Can Bind a Broad Range Of Divalent Metalsmentioning

confidence: 96%

“…Previous structures of cluster A-1 SBPs showed four metal-coordinating amino acids, either two His and two carboxylates (Glu/Asp) or three His and one carboxylate (Asp) leading to a tetrahedral or a highly distorted octahedral geometry [18,19]. Previous structures of cluster A-1 SBPs showed four metal-coordinating amino acids, either two His and two carboxylates (Glu/Asp) or three His and one carboxylate (Asp) leading to a tetrahedral or a highly distorted octahedral geometry [18,19].…”

Section: Comparison With Orthologuesmentioning

confidence: 99%

“…Using DSC and ITC, we showed that FpvC-like calprotectin is polyspecific and can bind different divalent metal including Fe 2+ , Mn 2+ , Ni 2+ and Zn 2+ . Prior works on cluster A-1 SBPs (PsaA, ZnuA, TroA and the most recent on YfeA) showed that these proteins are also capable of interaction with a broad range of metal ions and thus appear to be polyselective [18][19][20]29]. This result seems not in agreement with the Irving-Williams series [23] (Mg 2+ < Mn 2+ < Fe 2+ < Co 2+ < Ni 2+ < Cu 2+ < Zn 2+) showing that in the case of FpvC, Mn 2+ and Ni 2+ are thermodynamically favoured over Zn 2+ for an octahedral coordination site.…”

Section: Large Conformational Changes Upon Ligand Bindingmentioning

confidence: 99%

“…The best match concerns the structure of YfeA from Yersinia pestis (PDB 5UYE[18] with a RMSD of 2.2 The best match concerns the structure of YfeA from Yersinia pestis (PDB 5UYE[18] with a RMSD of 2.2…”

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confidence: 99%

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A unique ferrous iron binding mode is associated with large conformational changes for the transport protein FpvC of Pseudomonas aeruginosa

et al. 2019

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Pseudomonas aeruginosa secretes pyoverdine, a major siderophore to get access to iron, an essential nutrient. Pyoverdine scavenges ferric iron in the bacterial environment with the resulting complex internalized by bacteria. Releasing of iron from pyoverdine in the periplasm involves an iron reduction by an inner membrane reductase and two solute‐binding proteins (SBPs) FpvC and FpvF in association with their ABC transporter. FpvC and FpvF belong to two different subgroups of SBPs within the structural cluster A: FpvC and FpvF were proposed to be a metal‐binding protein and a ferrisiderophore‐binding protein respectively. Here, we report the redox state and the binding mode of iron to FpvC. We first solved the crystal structure of FpvC bound to a fortuitous Ni2+ by single anomalous dispersion method. Using a different protein purification strategy, we determined the structure of FpvC with manganese and iron, which binds to FpvC in a ferrous state as demonstrated by electron paramagnetic resonance. FpvC is the first example of a hexahistidine metal site among SBPs in which the Fe2+ redox state is stabilized under aerobic conditions. Using biophysics methods, we showed that FpvC reversibly bind to a broad range of divalent ions. The structure of a mutant mimicking the apo FpvC reveals a protein in an open state with large conformational changes when compared with the metal‐bound FpvC. These results highlight that the canonical metal site in FpvC is distinct from those yet described in SBPs and they provide new insights into the mechanism of PVD‐Fe dissociation in P. aeruginosa.

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Section: Fpvc Can Bind a Broad Range Of Divalent Metalsmentioning

confidence: 96%

Section: Comparison With Orthologuesmentioning

confidence: 99%

Section: Large Conformational Changes Upon Ligand Bindingmentioning

confidence: 99%

mentioning

confidence: 99%

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A unique ferrous iron binding mode is associated with large conformational changes for the transport protein FpvC of Pseudomonas aeruginosa

et al. 2019

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“…Burkholderia pseudomallei, B. mallei, and B. thailandensis also primarily infect patients with disorders that lead to compromised immune systems, such as persons with cystic fibrosis (Sawana et al, 2014). These three bacteria share many gene clusters involved in predicted polyketide synthase or nonribosomal peptide synthetase genes that are closely associated with the synthesis of natural products, including siderophores, which play key roles in the progression and propagation of infection (Radka et al, 2017).…”

Section: Innovative Applications Of Siderophores In Deciphering Tmentioning

confidence: 99%

Mass spectrometry and associated technologies delineate the advantageously biomedical capacity of siderophores in different pathogenic contexts

Luo

Guo

et al. 2018

Mass Spectrometry Reviews

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Siderophores are chemically diverse small molecules produced by microorganisms for chelation of irons to maintain their survival and govern some important biological functions, especially those cause that infections in hosts. Still, siderophores can offer new insight into a better understanding of the diagnosis and treatments of infectious diseases from the siderophore biosynthesis and regulation perspective. Thus, this review aims to summarize the biomedical value and applicability of siderophores in pathogenic contexts by briefly reviewing mass spectrometry (MS)-based chemical biology and translational applications that involve diagnosis, pathogenesis, and therapeutic discovery for a variety of infectious conditions caused by different pathogens. We highlight the advantages and disadvantages of siderophore discovery and applications in pathogenic contexts. Finally, we propose a panel of new and promising strategy as precision-modification metabolomics method, to rapidly advance the discovery of and translational innovations pertaining to these value compounds in broad biomedical niches. © 2018 Wiley Periodicals, Inc. Mass Spec Rev XX:XX-XX, 2018.

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Structural and functional insights into iron acquisition from lactoferrin and transferrin in Gram-negative bacterial pathogens

Chan

Fraser

et al. 2022

Biometals

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Iron is an essential element for various lifeforms but is largely insoluble due to the oxygenation of Earth’s atmosphere and oceans during the Proterozoic era. Metazoans evolved iron transport glycoproteins, like transferrin (Tf) and lactoferrin (Lf), to keep iron in a non-toxic, usable form, while maintaining a low free iron concentration in the body that is unable to sustain bacterial growth. To survive on the mucosal surfaces of the human respiratory tract where it exclusively resides, the Gram-negative bacterial pathogen Moraxella catarrhalis utilizes surface receptors for acquiring iron directly from human Tf and Lf. The receptors are comprised of a surface lipoprotein to capture iron-loaded Tf or Lf and deliver it to a TonB-dependent transporter (TBDT) for removal of iron and transport across the outer membrane. The subsequent transport of iron into the cell is normally mediated by a periplasmic iron-binding protein and inner membrane transport complex, which has yet to be determined for Moraxella catarrhalis. We identified two potential periplasm to cytoplasm transport systems and performed structural and functional studies with the periplasmic binding proteins (FbpA and AfeA) to evaluate their role. Growth studies with strains deleted in the fbpA or afeA gene demonstrated that FbpA, but not AfeA, was required for growth on human Tf or Lf. The crystal structure of FbpA with bound iron in the open conformation was obtained, identifying three tyrosine ligands that were required for growth on Tf or Lf. Computational modeling of the YfeA homologue, AfeA, revealed conserved residues involved in metal binding.

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Crystal structure ofYersinia pestisvirulence factor YfeA reveals two polyspecific metal-binding sites

Cited by 17 publications

References 50 publications

A unique ferrous iron binding mode is associated with large conformational changes for the transport protein FpvC of Pseudomonas aeruginosa

A unique ferrous iron binding mode is associated with large conformational changes for the transport protein FpvC of Pseudomonas aeruginosa

Mass spectrometry and associated technologies delineate the advantageously biomedical capacity of siderophores in different pathogenic contexts

Structural and functional insights into iron acquisition from lactoferrin and transferrin in Gram-negative bacterial pathogens

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