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. 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 substrat

SUBMITTER: Radka CD 

PROVIDER: S-EPMC5505154 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature