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Protein plasticity to the extreme: changing the topology of a 4-alpha-helical bundle with a single amino acid substitution.

Glykos NM, Cesareni G, Kokkinidis M
Structure 7 597-603 (1999)
Cited: 32 times
EuropePMC logo PMID: 10404589

Abstract

Background
Results

We have determined the high-resolution crystal structure of a 4-alpha-helical protein with a single alanine to proline mutation in the turn region, and show that this single amino acid substitution leads to a complete reorganisation of the whole molecule. The protein is converted from the canonical left-handed all-antiparallel form, to a right-handed mixed parallel and antiparallel bundle, which to the best of our knowledge and belief represents a novel topological motif for this class of proteins.

Conclusion

The results suggest a possible new mechanism for the creation and evolution of topological motifs, show the importance of loop regions in determining the allowable folding pathways, and illustrate the malleability of protein structures.

Articles - 1b6q mentioned but not cited (4)

  1. Bhageerath: an energy based web enabled computer software suite for limiting the search space of tertiary structures of small globular proteins. Jayaram B, Bhushan K, Shenoy SR, Narang P, Bose S, Agrawal P, Sahu D, Pandey V. Nucleic Acids Res 34 6195-6204 (2006)
  2. Structural plasticity of 4-α-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein. Amprazi M, Kotsifaki D, Providaki M, Kapetaniou EG, Fellas G, Kyriazidis I, Pérez J, Kokkinidis M. Proc Natl Acad Sci U S A 111 11049-11054 (2014)
  3. Structuprint: a scalable and extensible tool for two-dimensional representation of protein surfaces. Kontopoulos DG, Vlachakis D, Tsiliki G, Kossida S. BMC Struct Biol 16 4 (2016)
  4. Design and Selection of Heterodimerizing Helical Hairpins for Synthetic Biology. Smith AJ, Naudin EA, Edgell CL, Baker EG, Mylemans B, FitzPatrick L, Herman A, Rice HM, Andrews DM, Tigue N, Woolfson DN, Savery NJ. ACS Synth Biol 12 1845-1858 (2023)


Reviews citing this publication (8)

  1. De novo design of helical bundles as models for understanding protein folding and function. Hill RB, Raleigh DP, Lombardi A, DeGrado WF. Acc Chem Res 33 745-754 (2000)
  2. More than the sum of their parts: on the evolution of proteins from peptides. Söding J, Lupas AN. Bioessays 25 837-846 (2003)
  3. Evolution of protein structures and functions. Kinch LN, Grishin NV. Curr Opin Struct Biol 12 400-408 (2002)
  4. Coiled-coils in type III secretion systems: structural flexibility, disorder and biological implications. Gazi AD, Charova SN, Panopoulos NJ, Kokkinidis M. Cell Microbiol 11 719-729 (2009)
  5. Energetics of oligomeric protein folding and association. Doyle CM, Rumfeldt JA, Broom HR, Broom A, Stathopulos PB, Vassall KA, Almey JJ, Meiering EM. Arch Biochem Biophys 531 44-64 (2013)
  6. Combinatorial approaches to protein stability and structure. Magliery TJ, Regan L. Eur J Biochem 271 1595-1608 (2004)
  7. Genetic variation in CYP3A43 is associated with response to antipsychotic medication. Brandl EJ, Chowdhury NI, Tiwari AK, Lett TA, Meltzer HY, Kennedy JL, Müller DJ. J Neural Transm (Vienna) 122 29-34 (2015)
  8. α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles. Gazi AD, Kokkinidis M, Fadouloglou VE. Int J Mol Sci 22 5412 (2021)

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