Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Sodium-Coupled Secondary Transporters, Structure and Function

Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_248

Synonyms

Definition

Secondary active transporters are membrane proteins that move a substrate (main substrate) across the cell membrane against its concentration gradient, utilizing the free energy stored in the downhill concentration gradient of one or more coupled substrates, usually ions. Active, in contrast to passive, indicates that the movement of the main substrate is against its concentration gradient, in other words, uphill. Secondary, in contrast to primary, indicates that the energy source of the active transport is not directly from the hydrolysis of ATP (adenosine triphosphate), instead the transporter utilizes a gradient established by a primary transporter, which is often ATP requiring.

Na+-coupled secondary transporters refer to secondary active transporters that utilize the free energy stored in the electrochemical potential difference of sodium ions in and out of the cell membrane. This...

This is a preview of subscription content, log in to check access

References

  1. Abramson J, Wright EM (2009) Structure and function of Na+-symporters with inverted repeats. Curr Opin Struct Biol 19:425–432CrossRefPubMedGoogle Scholar
  2. Forrest LR, Kramer R, Ziegler C (2011) The structural basis of secondary active transport mechanisms. Biochim Biophys Acta 1807:167–188CrossRefPubMedGoogle Scholar
  3. Forrest LR, Tavoulari S, Zhang YW, Rudnick G, Honig B (2007) Identification of a chloride ion binding site in Na+/Cl–dependent transporters. Proc Nat Acad Sci USA 104:12761–12766CrossRefPubMedGoogle Scholar
  4. Jardetzk O (1966) Simple allosteric model for membrane pumps. Nature 211:969–970CrossRefGoogle Scholar
  5. Krishnamurthy H, Piscitelli CL, Gouaux E (2009) Unlocking the molecular secrets of sodium-coupled transporters. Nature 459:347–355CrossRefPubMedGoogle Scholar
  6. Reyes N, Ginter C, Boudker O (2009) Transport mechanism of a bacterial homologue of glutamate transporters. Nature 462:880–885CrossRefPubMedGoogle Scholar
  7. Shimamura T, Weyand S, Beckstein O, Rutherford NG, Hadden JM, Sharples D, Sansom MSP, Iwata S, Henderson PJF, Cameron AD (2010) Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1. Science 328:470–473CrossRefPubMedGoogle Scholar
  8. Yamashita A, Singh SK, Kawate T, Jin Y, Gouaux E (2005) Crystal structure of a bacterial homologue of Na+/Cl–dependent neurotransmitter transporters. Nature 437:215–223CrossRefPubMedGoogle Scholar
  9. Yernool D, Boudker O, Jin Y, Gouaux E (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431:811–818CrossRefPubMedGoogle Scholar
  10. Zhao CF, Noskov SY (2011) The role of local hydration and hydrogen-bonding dynamics in ion and solute release from Ion-coupled secondary transporters. Biochemistry 50:1848–1856CrossRefPubMedGoogle Scholar
  11. Zhao YF, Terry D, Shi L, Weinstein H, Blanchard SC, Javitch JA (2010) Single-molecule dynamics of gating in a neurotransmitter transporter homologue. Nature 465:188–U173CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Institute for Biocomplexity and Informatics and Department of Biological SciencesUniversity of CalgaryCalgaryCanada