Mechanisms of zinc binding to the solute-binding protein AztC and transfer from the metallochaperone AztD.

ABSTRACT: Bacteria can acquire the essential metal zinc from extremely zinc-limited environments by using ATP-binding cassette (ABC) transporters. These transporters are critical virulence factors, relying on specific and high-affinity binding of zinc by a periplasmic solute-binding protein (SBP). As such, the mechanisms of zinc binding and release among bacterial SBPs are of considerable interest as antibacterial drug targets. Zinc SBPs are characterized by a flexible loop near the high-affinity zinc-binding site. The function of this structure is not always clear, and its flexibility has thus far prevented structural characterization by X-ray crystallography. Here, we present intact structures for the zinc-specific SBP AztC from the bacterium Paracoccus denitrificans in the zinc-bound and a

SUBMITTER: Neupane DP 

PROVIDER: S-EPMC5655524 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature