Dataset Information


Structure and transport mechanism of the bacterial oxalate transporter OxlT.

ABSTRACT: Membrane proteins that belong to the major facilitator superfamily (MFS) are found in organisms across the evolutionary spectrum and mediate the transport of a variety of substrates ranging from small metabolites to neurotransmitters. The oxalate transporter (OxlT) is a representative MFS protein, and exchanges formate for oxalate across the cytoplasmic membrane of the organism Oxalobacter formigenes. Here, we present a structural model for the protein conformational changes that occur during oxalate transport by combining a three-dimensional map of the oxalate-bound, "closed" state of OxlT at 6.5 A determined by cryo-electron microscopy with a model of the "open" state of OxlT based on the atomic structures of the related transporters, glycerol-3-phosphate transporter (GlpT) and lactose permease (LacY). We demonstrate that the principal structural change associated with substrate transport is a concerted rocking movement of the two structurally similar halves of the protein relative to each other. Our structural model places two positively charged residues, Arg-272 and Lys-355 in the central cavity, suggesting that electrostatic interactions between these residues and the oxalate anion is a key step in generating the conformational change between the open and closed states of the transporter.


PROVIDER: S-EPMC1304825 | BioStudies | 2004-01-01

REPOSITORIES: biostudies

Similar Datasets

2017-01-01 | S-EPMC5328155 | BioStudies
2019-01-01 | S-EPMC6612311 | BioStudies
2019-01-01 | S-EPMC6797538 | BioStudies
1000-01-01 | S-EPMC4270380 | BioStudies
2016-01-01 | S-EPMC5083200 | BioStudies
2008-01-01 | S-EPMC2293189 | BioStudies
2011-01-01 | S-EPMC3143112 | BioStudies
2016-01-01 | S-EPMC5052600 | BioStudies
2017-01-01 | S-EPMC5535072 | BioStudies
2015-01-01 | S-EPMC4348557 | BioStudies