Skip to main content
Log in

1H, 15N and 13C resonance assignments of a repetitive domain of tubuliform spidroin 2

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

Spider silk is renowned for its excellent mechanical properties. Among six types of silk and one silk glue produced by different abdominal glands for various purposes, tubuliform (eggcase) silk is unique due to its high serine and low glycine content. Eggcase silk is spun from at least two spidroins, tubuliform spidroin 1 (TuSp1) and TuSp2. TuSp1 and TuSp2 were identified as the major and the minor components in tubuliform glands, respectively. TuSp2 consists of multiple repetitive (RP) domains with short terminal tails and shares very limited homology to all known spidroins. Here we report backbone and side chain resonance assignments of TuSp2-RP as a basis for structural and functional studies on eggcase silk formation.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2

Similar content being viewed by others

References

  • Ayoub NA, Garb JE, Tinghitella RM, Collin MA, Hayashi CY (2007) Blueprint for a high-performance biomaterial: full-length spider dragline silk genes. PLoS ONE 2:e514

    Article  ADS  Google Scholar 

  • Colgin MA, Lewis RV (1998) Spider minor ampullate silk proteins contain new repetitive sequences and highly conserved non-silk-like “spacer regions.” Protein Sci 7:667–672

    Article  Google Scholar 

  • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293

    Article  Google Scholar 

  • Garb JE, Hayashi CY (2005) Modular evolution of egg case silk genes across orb-weaving spider superfamilies. Proc Natl Acad Sci USA 102:11379–11384

    Article  ADS  Google Scholar 

  • Gosline JM, Guerette PA, Ortlepp CS, Savage KN (1999) The mechanical design of spider silks: from fibroin sequence to mechanical function. J Exp Biol 202:3295–3303

    Article  Google Scholar 

  • Huang W, Lin Z, Sin YM, Li D, Gong Z, Yang D (2006) Characterization and expression of a cDNA encoding a tubuliform silk protein of the golden web spider Nephila antipodiana. Biochimie 88:849–858

    Article  Google Scholar 

  • Huang W, Zhang Y, Chen Y, Wang Y, Yuan W, Zhang N, Lam TJ, Gong Z, Yang D, Lin Z (2017) From EST to novel spider silk gene identification for production of spidroin-based biomaterials. Sci Rep 7:13354

    Article  ADS  Google Scholar 

  • Johnson BA (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 278:313–352

    Google Scholar 

  • Lin Z, Xu YQ, Yang S, Yang D (2006) Sequence-specific assignment of aromatic resonances of uniformly 13C, 15N-labeled proteins by using 13C- and 15N-edited NOESY spectra. Angew Chem Int Ed Eng l45:1960–1963

    Article  Google Scholar 

  • Lin Z, Huang W, Zhang J, Fan JS, Yang D (2009) Solution structure of eggcase silk protein and its implications for silk fiber formation. Proc Natl Acad Sci USA 106:8906–8911

    Article  ADS  Google Scholar 

  • Viney C (2000) From natural silks to new polymer fibres. J Text Inst 91:2–23

    Article  Google Scholar 

  • Wen R, Wang K, Meng Q (2020) The three novel complete aciniform spidroin variants from Araneus ventricosus reveal diversity of gene sequences within specific spidroin type. Int J Biol Macromol 157:60–66

    Article  Google Scholar 

  • Wishart DS, Bigam CG, Holm A, Hodges RS, Sykes BD (1995) 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J Biomol NMR 5:67–81

    Article  Google Scholar 

  • Xu Y, Lin Z, Ho C, Yang D (2005) A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C, 15N-labeled large proteins. J Am Chem Soc 127:11920–11921

    Article  Google Scholar 

Download references

Acknowledgements

This work was supported by Grants from the National Natural Science Foundation of China (21974093 to Z.L.).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Zhi Lin.

Ethics declarations

Conflict of interest

The author declares that they have no conflict of interest.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Fan, T., Zhang, Y., Fan, JS. et al. 1H, 15N and 13C resonance assignments of a repetitive domain of tubuliform spidroin 2. Biomol NMR Assign 15, 475–477 (2021). https://doi.org/10.1007/s12104-021-10048-1

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-021-10048-1

Keywords

Navigation