This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Aconitase
From Proteopedia
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
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Ralf Stephan, David Canner, Joel L. Sussman, Jaime Prilusky, Anthony Noles, Angel Herraez, Eran Hodis
