Aconitase
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'''Rocker-switch type Major Facilitator antiporters''' are membrane proteins that facilitate both influx and outflux of specific small molecules in a way that is neither the passive letting-through of channels, nor the active pumping of ATPases. They tilt between the two states 'outside open' and 'inside open' and the tilting (or switching) movement does the transport if a molecule has docked beforehand. We call them antiport because, with the second switching back, usually a second, different, molecule is transported in the opposite direction. | '''Rocker-switch type Major Facilitator antiporters''' are membrane proteins that facilitate both influx and outflux of specific small molecules in a way that is neither the passive letting-through of channels, nor the active pumping of ATPases. They tilt between the two states 'outside open' and 'inside open' and the tilting (or switching) movement does the transport if a molecule has docked beforehand. We call them antiport because, with the second switching back, usually a second, different, molecule is transported in the opposite direction. | ||
| - | The glpT subfamily of transporters consist of several transport proteins from bacteria like ''E. coli'' and ''Salmonella typhimurium'', but also the human glucose-6-phosphate translocase. They all are evolutionary connected and have 12 transmembrane helices that stand together to make an opening between them, like a channel. This channel, however, is closed for any molecule in the empty configuration of the molecule.<ref>PMID:18537473</ref><ref>PMID:12893936</ref> | + | The glpT subfamily of transporters consist of several transport proteins from bacteria like ''E. coli'' and ''Salmonella typhimurium'', but also the human glucose-6-phosphate translocase. They all are evolutionary connected and have 12 transmembrane helices that stand together to make an opening between them, like a channel. This channel, however, is closed for any molecule in the empty configuration of the molecule.<ref>PMID:18537473</ref><ref>PMID:17915951</ref><ref>PMID:12893936</ref> |
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:04, 6 February 2009
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Rocker-switch type Major Facilitator antiporters are membrane proteins that facilitate both influx and outflux of specific small molecules in a way that is neither the passive letting-through of channels, nor the active pumping of ATPases. They tilt between the two states 'outside open' and 'inside open' and the tilting (or switching) movement does the transport if a molecule has docked beforehand. We call them antiport because, with the second switching back, usually a second, different, molecule is transported in the opposite direction.
The glpT subfamily of transporters consist of several transport proteins from bacteria like E. coli and Salmonella typhimurium, but also the human glucose-6-phosphate translocase. They all are evolutionary connected and have 12 transmembrane helices that stand together to make an opening between them, like a channel. This channel, however, is closed for any molecule in the empty configuration of the molecule.[1][2][3]
References
- ↑ Law CJ, Maloney PC, Wang DN. Ins and outs of major facilitator superfamily antiporters. Annu Rev Microbiol. 2008;62:289-305. PMID:18537473 doi:http://dx.doi.org/10.1146/annurev.micro.61.080706.093329
- ↑ Law CJ, Yang Q, Soudant C, Maloney PC, Wang DN. Kinetic evidence is consistent with the rocker-switch mechanism of membrane transport by GlpT. Biochemistry. 2007 Oct 30;46(43):12190-7. Epub 2007 Oct 4. PMID:17915951 doi:http://dx.doi.org/10.1021/bi701383g
- ↑ Huang Y, Lemieux MJ, Song J, Auer M, Wang DN. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science. 2003 Aug 1;301(5633):616-20. PMID:12893936 doi:10.1126/science.1087619
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