Skip to main content

Thank you for visiting 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.

The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A


Eukaryotic translation initiation factors (eIFs) 1A and 1 are central players in the complex process of start-codon recognition. To improve mechanistic understanding of this process, we determined the crystal structure of the 40S ribosomal subunit in complex with eIF1A and eIF1 from Tetrahymena thermophila at a resolution of 3.7 Å. It reveals the positions of the two factors on the 40S and the conformational changes that accompany their binding.

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

Relevant articles

Open Access articles citing this article.

Access options

Buy article

Get time limited or full article access on ReadCube.


All prices are NET prices.

Figure 1: eIF1A and eIF1 bound to the 40S subunit.
Figure 2: Rearrangements and interactions in the 40S–eIF1–eIF1A complex.

Accession codes

Primary accessions

Protein Data Bank

Referenced accessions

Protein Data Bank



  1. Hinnebusch, A.G. & Lorsch, J.R. Cold Spring Harb. Perspect. Biol. 4, a011544 (2012).

    Article  Google Scholar 

  2. Pestova, T.V., Borukhov, S.I. & Hellen, C.U. Nature 394, 854–859 (1998).

    CAS  Article  Google Scholar 

  3. Fekete, C.A. et al. EMBO J. 24, 3588–3601 (2005).

    CAS  Article  Google Scholar 

  4. Nanda, J.S. et al. J. Mol. Biol. 394, 268–285 (2009).

    CAS  Article  Google Scholar 

  5. Acker, M.G., Shin, B.S., Dever, T.E. & Lorsch, J.R. J. Biol. Chem. 281, 8469–8475 (2006).

    CAS  Article  Google Scholar 

  6. Rabl, J., Leibundgut, M., Ataide, S.F., Haag, A. & Ban, N. Science 331, 730–736 (2011).

    CAS  Article  Google Scholar 

  7. Battiste, J.L., Pestova, T.V., Hellen, C.U. & Wagner, G. Mol. Cell 5, 109–119 (2000).

    CAS  Article  Google Scholar 

  8. Yu, Y. et al. Nucleic Acids Res. 37, 5167–5182 (2009).

    CAS  Article  Google Scholar 

  9. Ben-Shem, A. et al. Science 334, 1524–1529 (2011).

    CAS  Article  Google Scholar 

  10. Carter, A.P. et al. Science 291, 498–501 (2001).

    CAS  Article  Google Scholar 

  11. Saini, A.K., Nanda, J.S., Lorsch, J.R. & Hinnebusch, A.G. Genes Dev. 24, 97–110 (2010).

    CAS  Article  Google Scholar 

  12. Olsen, D.S. et al. EMBO J. 22, 193–204 (2003).

    CAS  Article  Google Scholar 

  13. Marintchev, A., Kolupaeva, V.G., Pestova, T.V. & Wagner, G. Proc. Natl. Acad. Sci. USA 100, 1535–1540 (2003).

    CAS  Article  Google Scholar 

  14. Ogle, J.M. et al. Science 292, 897–902 (2001).

    CAS  Article  Google Scholar 

  15. Maag, D. & Lorsch, J.R. J. Mol. Biol. 330, 917–924 (2003).

    CAS  Article  Google Scholar 

  16. Qin, D. & Fredrick, K. Mol. Microbiol. 71, 1239–1249 (2009).

    CAS  Article  Google Scholar 

  17. Shin, B.S. et al. Nat. Struct. Mol. Biol. 18, 1227–1234 (2011).

    CAS  Article  Google Scholar 

  18. Passmore, L.A. et al. Mol. Cell 26, 41–50 (2007).

    CAS  Article  Google Scholar 

  19. Fekete, C.A. et al. EMBO J. 26, 1602–1614 (2007).

    CAS  Article  Google Scholar 

  20. Voorhees, R.M., Weixlbaumer, A., Loakes, D., Kelley, A.C. & Ramakrishnan, V. Nat. Struct. Mol. Biol. 16, 528–533 (2009).

    CAS  Article  Google Scholar 

  21. Kabsch, W. Acta Crystallogr. D Biol. Crystallogr. 66, 125–132 (2010).

    CAS  Article  Google Scholar 

  22. Karplus, P.A. & Diederichs, K. Science 336, 1030–1033 (2012).

    CAS  Article  Google Scholar 

  23. McCoy, A.J. et al. J. Appl. Crystallogr. 40, 658–674 (2007).

    CAS  Article  Google Scholar 

  24. Adams, P.D. et al. Acta Crystallogr. D Biol. Crystallogr. 58, 1948–1954 (2002).

    Article  Google Scholar 

  25. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Acta Crystallogr. A 47, 110–119 (1991).

    Article  Google Scholar 

  26. Emsley, P., Lohkamp, B., Scott, W.G. & Cowtan, K. Acta Crystallogr. D Biol. Crystallogr. 66, 486–501 (2010).

    CAS  Article  Google Scholar 

  27. Laskowski, R.A., Rullmannn, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. J. Biomol. NMR 8, 477–486 (1996).

    CAS  Article  Google Scholar 

  28. Baker, N.A., Sept, D., Joseph, S., Holst, M.J. & McCammon, J.A. Proc. Natl. Acad. Sci. USA 98, 10037–10041 (2001).

    CAS  Article  Google Scholar 

  29. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. & Lipman, D.J. J. Mol. Biol. 215, 403–410 (1990).

    CAS  Article  Google Scholar 

  30. Larkin, M.A. et al. Bioinformatics 23, 2947–2948 (2007).

    CAS  Article  Google Scholar 

  31. Waterhouse, A.M., Procter, J.B., Martin, D.M., Clamp, M. & Barton, G.J. Bioinformatics 25, 1189–1191 (2009).

    CAS  Article  Google Scholar 

  32. Bond, C.S. & Schuttelkopf, A.W. Acta Crystallogr. D Biol. Crystallogr. 65, 510–512 (2009).

    CAS  Article  Google Scholar 

  33. Klinge, S., Voigts-Hoffmann, F., Leibundgut, M. & Ban, N. Trends Biochem. Sci. 37, 189–198 (2012).

    CAS  Article  Google Scholar 

Download references


All data were collected at the Swiss Light Source (SLS, Paul Scherrer Institut, Villigen). We thank T. Tomizaki, M. Müller, V. Olieric, M. Wang, C. Pradervand, M. Marsh and A. Pauluhn for their outstanding support at the SLS; A. Haag for advice on cell growth, ribosome purification and eIF cloning and purification; V. Hozjan and F. Benning for experimental support; and D. Böhringer, B. Greber and A. Casañas for critical reading of the manuscript. This work was supported by the Swiss National Science Foundation (SNSF) (grant 31003A 144214 to N.B.), the National Center of Excellence in Research Structural Biology program of the SNSF (N.B.) and the European Community's Seventh Framework Programme (Project PF7 250071 to N.B.).

Author information

Authors and Affiliations



J.R. cloned the initiation factors. M.W. and J.R. purified the initiation factors. M.W. crystallized the eIF1–eIF1A–40S complex. M.W. and M.L. solved the crystal structure. M.W., M.L., F.V.-H. and N.B. analyzed the data, interpreted the structure and wrote the manuscript.

Corresponding author

Correspondence to Nenad Ban.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Supplementary information

Supplementary Text and Figures

Supplementary Figures 1–5 and Supplementary Tables 1–3 (PDF 10686 kb)

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Weisser, M., Voigts-Hoffmann, F., Rabl, J. et al. The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A. Nat Struct Mol Biol 20, 1015–1017 (2013).

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI:

Further reading


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