Structural basis for the alternating access mechanism of the cation diffusion facilitator YiiP.

ABSTRACT: YiiP is a dimeric antiporter from the cation diffusion facilitator family that uses the proton motive force to transport Zn²⁺ across bacterial membranes. Previous work defined the atomic structure of an outward-facing conformation, the location of several Zn²⁺ binding sites, and hydrophobic residues that appear to control access to the transport sites from the cytoplasm. A low-resolution cryo-EM structure revealed changes within the membrane domain that were associated with the alternating access mechanism for transport. In the current work, the resolution of this cryo-EM structure has been extended to 4.1 Å. Comparison with the X-ray structure defines the differences between inward-facing and outward-facing conformations at an atomic level. These differences include

SUBMITTER: Lopez-Redondo ML 

PROVIDER: S-EPMC5866550 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature