Shared Molecular Mechanisms of Membrane Transporters. Review uri icon

Overview

abstract

  • The determination of the crystal structures of small-molecule transporters has shed light on the conformational changes that take place during structural isomerization from outward- to inward-facing states. Rather than using a simple rocking movement of two bundles around a central substrate-binding site, it has become clear that even the most simplistic transporters utilize rearrangements of nonrigid bodies. In the most dramatic cases, one bundle is fixed while the other, structurally divergent, bundle carries the substrate some 18 Å across the membrane, which in this review is termed an elevator alternating-access mechanism. Here, we compare and contrast rocker-switch, rocking-bundle, and elevator alternating-access mechanisms to highlight shared features and novel refinements to the basic alternating-access model.

publication date

  • March 21, 2016

Research

keywords

  • Escherichia coli
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • Molecular Dynamics Simulation

Identity

Scopus Document Identifier

  • 84974678467

Digital Object Identifier (DOI)

  • 10.1146/annurev-biochem-060815-014520

PubMed ID

  • 27023848

Additional Document Info

volume

  • 85