Work

Ins and Outs of Major Facilitator Superfamily Antiporters

Year: 2008

Type: review

Abstract: The major facilitator superfamily (MFS) represents the largest group of secondary active membrane transporters, and its members transport a diverse range of substrates. Recent work shows that MFS antiporters, and perhaps all members of the MFS, share the same three-dimensional structure, consisting of two domains that surround a substrate translocation pore. The advent of crystal structures of three MFS antiporters sheds light on their fundamental mechanism; they operate via a single binding site, alternating-access mechanism that involves a rocker-switch type movement of the two halves of the protein. In the sn-glycerol-3-phosphate transporter (GlpT) from Escherichia coli, the substrate-binding site is formed by several charged residues and a histidine that can be protonated. Salt-bridge formation and breakage are involved in the conformational changes of the protein during transport. In this review, we attempt to give an account of a set of mechanistic principles that characterize all MFS antiporters.

Source: Annual Review of Microbiology

DOI: 10.1146/annurev.micro.61.080706.093329

Authors: Christopher J. Law, Peter C. Maloney, Da-Neng Wang

Institutions: New York University, Johns Hopkins University, Johns Hopkins Medicine

Language: English

Topic: Drug Transport and Resistance Mechanisms

Subfield: Oncology

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: Ion Gradients and Energy Coupling in Bacteria, G46975173, Ion Gradients and Energy Coupling in Bacteria, Structural Studies of Sugar Transporters