Skip to main content

Up, Down, and Around: Identifying Recurrent Interactions Within and Between Super-secondary Structures in β-Propellers

  • Protocol
  • First Online:
Protein Supersecondary Structures

Part of the book series: Methods in Molecular Biology ((MIMB,volume 932))

  • 1527 Accesses

Abstract

The examination and analysis of super-secondary structures or other specific structural patterns associated with particular functions, sequence motifs, or structural contexts require that the set of structures examined shares the same feature. This seems obvious but in practice this may often present problems such as identifying complete sets of data avoiding false positives. In the case of the β-propeller structures the symmetry of the propeller creates problems for many structure similarity search programs. Here we present a procedure that will identify propeller structures in PDB and assign them to the different N-propeller types. In addition we outline methods to examine similarities and differences within and between the four stranded up-and-down blades of the β-propeller.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Subscribe and save

Springer+ Basic
€32.70 /Month
  • Get 10 units per month
  • Download Article/Chapter or eBook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Protocol
EUR 44.95
Price includes VAT (Finland)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
EUR 93.08
Price includes VAT (Finland)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
EUR 120.99
Price includes VAT (Finland)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
EUR 164.99
Price includes VAT (Finland)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Similar content being viewed by others

References

  1. Orengo CA, Michie AD, Jones S et al (1997) CATH—a hierarchic classification of protein domain structures. Structure 5:1093–1108

    Article  PubMed  CAS  Google Scholar 

  2. Murzin AG, Brenner SE, Hubbard T et al (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247:536–540

    PubMed  CAS  Google Scholar 

  3. Rao ST, Rossmann MG (1973) Comparison of super-secondary structures in proteins. J Mol Biol 76:241–256

    Article  PubMed  CAS  Google Scholar 

  4. Varghese JN, Laver WG, Colman PM (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303:35–40

    Article  PubMed  CAS  Google Scholar 

  5. Murzin AG (1992) Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry. Proteins 14:191–201

    Article  PubMed  CAS  Google Scholar 

  6. Paoli M (2001) Protein folds propelled by diversity. Prog Biophys Mol Biol 76:103–130

    Article  PubMed  CAS  Google Scholar 

  7. Baker SC, Saunders NF, Willis AC et al (1997) Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds. J Mol Biol 269:440–455

    Article  PubMed  CAS  Google Scholar 

  8. Russell RB, Sasieni PD, Sternberg MJ (1998) Supersites within superfolds. Binding site similarity in the absence of homology. J Mol Biol 282:903–918

    Article  PubMed  CAS  Google Scholar 

  9. Quistgaard EM, Thirup SS (2009) Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families. BMC Struct Biol 9:46

    Article  PubMed  Google Scholar 

  10. Crennell S, Garman E, Laver G et al (1994) Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure 2:535–544

    Article  PubMed  CAS  Google Scholar 

  11. Nojiri M, Hira D, Yamaguchi K et al (2006) Crystal structures of cytochrome c(L) and methanol dehydrogenase from Hypho­microbium denitrificans: structural and mechanistic insights into interactions between the two proteins. Biochemistry 45:3481–3492

    Article  PubMed  CAS  Google Scholar 

  12. Mattei P, Boehringer M, Di Giorgio P et al (2010) Discovery of carmegliptin: a potent and long-acting dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes. Bioorg Med Chem Lett 20:1109–1113

    Article  PubMed  CAS  Google Scholar 

  13. Severi E, Muller A, Potts JR et al (2008) Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT. J Biol Chem 283:4841–4849

    Article  PubMed  CAS  Google Scholar 

  14. Jing H, Takagi J, Liu JH et al (2002) Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins. Structure 10:1453–1464

    Article  PubMed  CAS  Google Scholar 

  15. Springer TA (1998) An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components. J Mol Biol 283:837–862

    Article  PubMed  CAS  Google Scholar 

  16. Chaudhuri I, Soding J, Lupas AN (2008) Evolution of the beta-propeller fold. Proteins 71:795–803

    Article  PubMed  CAS  Google Scholar 

  17. Berman HM, Westbrook J, Feng Z et al (2000) The Protein Data Bank. Nucleic Acids Res 28:235–242

    Article  PubMed  CAS  Google Scholar 

  18. Finn RD, Mistry J, Tate J et al (2010) The Pfam protein families database. Nucleic Acids Res 38:D211–D222

    Article  PubMed  CAS  Google Scholar 

  19. Holm L, Rosenstrom P (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38:W545–W549

    Article  PubMed  CAS  Google Scholar 

  20. Velankar S, Alhroub Y, Alili A et al (2011) PDBe: Protein Data Bank in Europe. Nucleic Acids Res 39:D402–D410

    Article  PubMed  Google Scholar 

  21. Kleywegt GJ (1999) Recognition of spatial motifs in protein structures. J Mol Biol 285:1887–1897

    Article  PubMed  CAS  Google Scholar 

  22. Waterhouse AM, Procter JB, Martin DM et al (2009) Jalview Version 2–a multiple sequence alignment editor and analysis workbench. Bioinformatics 25:1189–1191

    Article  PubMed  CAS  Google Scholar 

  23. Konagurthu AS, Whisstock JC, Stuckey PJ et al (2006) MUSTANG: a multiple structural alignment algorithm. Proteins 64:559–574

    Article  PubMed  CAS  Google Scholar 

  24. Nurizzo D, Turkenburg JP, Charnock SJ et al (2002) Cellvibrio japonicus alpha-l-arabinanase 43A has a novel five-blade beta-propeller fold. Nat Struct Biol 9:665–668

    Article  PubMed  CAS  Google Scholar 

  25. Forouhar F, Abashidze M, Conover K et al (2005) unpublished

    Google Scholar 

  26. Williams PA, Fulop V, Garman EF et al (1997) Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme. Nature 389:406–412

    Article  PubMed  CAS  Google Scholar 

  27. Malby RL, McCoy AJ, Kortt AA et al (1998) Three-dimensional structures of single-chain Fv-neuraminidase complexes. J Mol Biol 279:901–910

    Article  PubMed  CAS  Google Scholar 

  28. Quistgaard EM, Madsen P, Groftehauge MK et al (2009) Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain. Nat Struct Mol Biol 16:96–98

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgments

We wish to thank The Lundbeck Foundation for financial support through the MIND Centre and The Danish National Research Foundation for funding through the CARB Centre.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Søren Thirup .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2012 Springer Science+Business Media New York

About this protocol

Cite this protocol

Thirup, S., Gupta, V., Quistgaard, E.M. (2012). Up, Down, and Around: Identifying Recurrent Interactions Within and Between Super-secondary Structures in β-Propellers. In: Kister, A. (eds) Protein Supersecondary Structures. Methods in Molecular Biology, vol 932. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-065-6_3

Download citation

  • DOI: https://doi.org/10.1007/978-1-62703-065-6_3

  • Published:

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-064-9

  • Online ISBN: 978-1-62703-065-6

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics