AlphaFold2 predicts the inward-facing conformation of the multidrug transporter LmrP

Proteins. 2021 Sep;89(9):1226-1228. doi: 10.1002/prot.26138. Epub 2021 May 18.

Abstract

As part of the CASP competition, the protein structure prediction algorithm AlphaFold2 generated multiple models of the proton/drug antiporter LmrP. Previous distance restraints from double electron-electron resonance spectroscopy, a technique which reports distance distributions between spin labels attached to proteins, suggest that one of the lower-ranked models may have captured a conformation that has so far eluded experimental structure determination.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Algorithms*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Biological Transport
  • Cell Membrane / chemistry*
  • Cell Membrane / metabolism
  • Gene Expression
  • Lactococcus lactis / chemistry*
  • Lactococcus lactis / genetics
  • Lactococcus lactis / metabolism
  • Membrane Transport Proteins / chemistry*
  • Membrane Transport Proteins / genetics
  • Membrane Transport Proteins / metabolism
  • Models, Molecular
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Protein Interaction Domains and Motifs
  • Protons
  • Software*

Substances

  • Bacterial Proteins
  • LmrP protein, Lactococcus lactis
  • Membrane Transport Proteins
  • Protons