Aconitase
From Proteopedia
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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. | ||
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== References == | == References == | ||
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Revision as of 17:32, 6 February 2009
Template:STRUCTURE 1pw4 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]
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
- ↑ 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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Michal Harel, Alexander Berchansky, Ralf Stephan, David Canner, Joel L. Sussman, Jaime Prilusky, Anthony Noles, Angel Herraez, Eran Hodis
