PDBsum entry 5uyh

Metal transport

PDB id: 5uyh

Contents

Protein chain

272 a.a.

Metals

_MN ×2

Waters ×179

PDB id:

5uyh

Name:

Metal transport

Title:

Yfea with metal bound to site 2 - mn wavelength

Structure:

Periplasmic chelated iron-binding protein yfea. Chain: a. Engineered: yes

Source:

Yersinia pestis. Organism_taxid: 632. Gene: yfea, ypo2439, y1897, yp_2227. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.99Å R-factor: 0.190 R-free: 0.235

Authors:

C.D.Radka,L.J.Delucas,S.G.Aller

Key ref:

C.D.Radka et al. (2017). Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sites. Acta Crystallogr D Struct Biol, 73, 557-572. PubMed id: 28695856

Date:

24-Feb-17 Release date: 12-Jul-17

Protein chain

Q56952  (YFEA_YERPE) -  Iron-binding protein YfeA from Yersinia pestis

Seq: 311 a.a.

Struc: 272 a.a.

Acta Crystallogr D Struct Biol 73:557-572 (2017)

PubMed id: 28695856

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

C.D.Radka, L.J.DeLucas, L.S.Wilson, M.B.Lawrenz, R.D.Perry, S.G.Aller.

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.