Structure and function of Na(+)-symporters with inverted repeats
- PMID: 19631523
- PMCID: PMC3496787
- DOI: 10.1016/j.sbi.2009.06.002
Structure and function of Na(+)-symporters with inverted repeats
Abstract
Symporters are membrane proteins that couple energy stored in electrochemical potential gradients to drive the cotransport of molecules and ions into cells. Traditionally, proteins are classified into gene families based on sequence homology and functional properties, for example the sodium glucose (SLC5 or Sodium Solute Symporter Family, SSS or SSF) and GABA (SLC6 or Neurotransmitter Sodium Symporter Family, NSS or SNF) symporter families [1-4]. Recently, it has been established that four Na(+)-symporter proteins with unrelated sequences have a common structural core containing an inverted repeat of 5 transmembrane (TM) helices [5(**)-8(**)]. Analysis of these four structures reveals that they reside in different conformations along the transport cycle providing atomic insight into the mechanism of sodium solute cotransport.
Figures




Similar articles
-
Identification of a second substrate-binding site in solute-sodium symporters.J Biol Chem. 2015 Jan 2;290(1):127-41. doi: 10.1074/jbc.M114.584383. Epub 2014 Nov 14. J Biol Chem. 2015. PMID: 25398883 Free PMC article.
-
The sodium/iodide symporter: state of the art of its molecular characterization.Biochim Biophys Acta. 2014 Jan;1838(1 Pt B):244-53. doi: 10.1016/j.bbamem.2013.08.013. Epub 2013 Aug 27. Biochim Biophys Acta. 2014. PMID: 23988430 Review.
-
State-dependent conformations of the translocation pathway in the tyrosine transporter Tyt1, a novel neurotransmitter:sodium symporter from Fusobacterium nucleatum.J Biol Chem. 2006 Sep 8;281(36):26444-54. doi: 10.1074/jbc.M602438200. Epub 2006 Jun 23. J Biol Chem. 2006. PMID: 16798738
-
The Na⁺/L-proline transporter PutP.Front Biosci (Landmark Ed). 2012 Jan 1;17(2):745-59. doi: 10.2741/3955. Front Biosci (Landmark Ed). 2012. PMID: 22201772 Review.
-
Function Trumps Form in Two Sugar Symporters, LacY and vSGLT.Int J Mol Sci. 2021 Mar 30;22(7):3572. doi: 10.3390/ijms22073572. Int J Mol Sci. 2021. PMID: 33808202 Free PMC article. Review.
Cited by
-
Regulation of Neutral Amino Acid Transport By the SARS-CoV-2 Receptor ACE2.Function (Oxf). 2021 Sep 4;2(5):zqab048. doi: 10.1093/function/zqab048. eCollection 2021. Function (Oxf). 2021. PMID: 34642665 Free PMC article. No abstract available.
-
Structural determinants of water permeation through the sodium-galactose transporter vSGLT.Biophys J. 2014 Mar 18;106(6):1280-9. doi: 10.1016/j.bpj.2014.01.006. Biophys J. 2014. PMID: 24655503 Free PMC article.
-
The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters.Physiology (Bethesda). 2009 Dec;24:377-86. doi: 10.1152/physiol.00030.2009. Physiology (Bethesda). 2009. PMID: 19996368 Free PMC article. Review.
-
ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein.Chem Biol. 2012 Feb 24;19(2):287-96. doi: 10.1016/j.chembiol.2011.11.009. Epub 2011 Dec 29. Chem Biol. 2012. PMID: 22209629 Free PMC article.
-
Topologically random insertion of EmrE supports a pathway for evolution of inverted repeats in ion-coupled transporters.J Biol Chem. 2010 May 14;285(20):15234-15244. doi: 10.1074/jbc.M110.108746. Epub 2010 Mar 22. J Biol Chem. 2010. PMID: 20308069 Free PMC article.
References
-
- Nelson N. The Family of Na+/C1- Neuortransmitter Transporters. Journal of Neurochemistry. 199871:1786–1803. - PubMed
-
- Wright EMaT E. The Sodium Glucose Cotransport Family SLC5. Pflugers Arch. 2004:510–518. - PubMed
-
- Turk E, Wright EM. Membrane topology motifs in the SGLT cotransporter family. J Membr Biol. 1997;159:1–20. - PubMed
-
- Chen NH, Reith ME, Quick MW. Synaptic uptake and beyond: the sodium-and chloride-dependent neurotransmitter transporter family SLC6. Pflugers Arch. 2004;447:519–531. - PubMed
-
- Yamashita A, Singh SK, Kawate T, Jin Y, Gouaux E. Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters. Nature. 2005;437:215–223. - PubMed
-
The first high resolution crystal structure of a sodium symporter with the inverted 5TM motif containing a pair of transmembrane discontinuous helices. The substrate, leucine, and one sodium was bound in a occluded site halfway across the membrane close to these two discontinuous helices. A route for substrate entry to the binding site from the external solution was identified and this conformation of the protein was termed the outward facing substrate occluded conformation.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources