Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

This is about the in and the out

At last, structures have been solved for different conformational states, facing in and facing out, for the same transporter protein of the major facilitator superfamily. The structural basis of alternating substrate access for binding and translocation can now be properly visualized.

This is a preview of subscription content, access via your institution

Relevant articles

Open Access articles citing this article.

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Figure 1: The sugar porter (SP) family and its relationship to other families in the major facilitator superfamily.
Figure 2: The three structures of XylE are represented from the plane of the membrane.
Figure 3

References

  1. Maiden, M.C. et al. Nature 325, 641–643 (1987).

    Article  CAS  Google Scholar 

  2. Pao, S.S. et al. Microbiol. Mol. Biol. Rev. 62, 1–34 (1998).

    CAS  PubMed  PubMed Central  Google Scholar 

  3. Reddy, V.S. et al. FEBS J. 279, 2022–2035 (2012).

    Article  CAS  Google Scholar 

  4. Mitchell, P. Biochem. Soc. Symp. 22, 142–169 (1963).

    Google Scholar 

  5. Jardetzky, O. Nature 211, 969–970 (1966).

    Article  CAS  Google Scholar 

  6. Boudker, O. & Verdon, G. Trends Pharmacol. Sci. 31, 418–426 (2012).

    Article  Google Scholar 

  7. Yan, N. Trends Biochem. Sci. 38, 151–159 (2013).

    Article  CAS  Google Scholar 

  8. Law, C.J. et al. Annu. Rev. Microbiol. 62, 289–305 (2008).

    Article  CAS  Google Scholar 

  9. Radestock, S. & Forrest, L.R. J. Mol. Biol. 407, 698–715 (2011).

    Article  CAS  Google Scholar 

  10. Sun, L. et al. Nature 490, 361–366 (2012).

    Article  CAS  Google Scholar 

  11. Madej, M.G. et al. Proc. Natl. Acad. Sci. USA 110, 5870–5874 (2013).

    Article  CAS  Google Scholar 

  12. Quistgaard, E.M. et al. Nat. Struct. Mol. Biol. 20, 766–768 (2013).

    Article  CAS  Google Scholar 

  13. Mirza, O. et al. EMBO J. 25, 1177–1183 (2006).

    Article  CAS  Google Scholar 

  14. Sanderson, N.M. et al. Biochem. Soc. Trans. 26, S306 (1998).

    Article  CAS  Google Scholar 

  15. Seyfang, A. et al. J. Biol. Chem. 272, 24210–24215 (1997).

    Article  CAS  Google Scholar 

  16. Pedersen, B.P. et al. Nature 496, 533–536 (2013).

    Article  CAS  Google Scholar 

  17. Martin, G.E. et al. J. Biol. Chem. 269, 24870–24877 (1994).

    CAS  PubMed  Google Scholar 

  18. Bettiga, M. et al. Biotech. Biofuels 1, 16 (2008).

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Peter J F Henderson.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Henderson, P., Baldwin, S. This is about the in and the out. Nat Struct Mol Biol 20, 654–655 (2013). https://doi.org/10.1038/nsmb.2604

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsmb.2604

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing