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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 289-305 |
| Number of pages | 17 |
| Journal | Annual Review of Microbiology |
| Volume | 62 |
| DOIs | |
| State | Published - 2008 |
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Keywords
- EmrD
- GlpT
- OxlT
- Rocker-switch mechanism
- Secondary membrane transporter proteins
- UhpT
ASJC Scopus subject areas
- Microbiology
Cite this
Ins and outs of major facilitator superfamily antiporters. / Law, Christopher J.; Maloney, Peter C.; Wang, Da Neng.
In: Annual Review of Microbiology, Vol. 62, 2008, p. 289-305.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ins and outs of major facilitator superfamily antiporters
AU - Law, Christopher J.
AU - Maloney, Peter C.
AU - Wang, Da Neng
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
KW - EmrD
KW - GlpT
KW - OxlT
KW - Rocker-switch mechanism
KW - Secondary membrane transporter proteins
KW - UhpT
UR - http://www.scopus.com/inward/record.url?scp=53849119555&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=53849119555&partnerID=8YFLogxK
U2 - 10.1146/annurev.micro.61.080706.093329
DO - 10.1146/annurev.micro.61.080706.093329
M3 - Article
C2 - 18537473
AN - SCOPUS:53849119555
VL - 62
SP - 289
EP - 305
JO - Annual Review of Microbiology
JF - Annual Review of Microbiology
SN - 0066-4227
ER -