2MU3

Spider wrapping silk fibre architecture arising from its modular soluble protein precursor


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Spider wrapping silk fibre architecture arising from its modular soluble protein precursor.

Tremblay, M.L.Xu, L.Lefevre, T.Sarker, M.Orrell, K.E.Leclerc, J.Meng, Q.Pezolet, M.Auger, M.Liu, X.Q.Rainey, J.K.

(2015) Sci Rep 5: 11502-11502

  • DOI: https://doi.org/10.1038/srep11502
  • Primary Citation of Related Structures:  
    2MU3

  • PubMed Abstract: 

    Spiders store spidroins in their silk glands as high concentration aqueous solutions, spinning these dopes into fibres with outstanding mechanical properties. Aciniform (or wrapping) silk is the toughest spider silk and is devoid of the short amino acid sequence motifs characteristic of the other spidroins. Using solution-state NMR spectroscopy, we demonstrate that the 200 amino acid Argiope trifasciata AcSp1 repeat unit contrasts with previously characterized spidroins, adopting a globular 5-helix bundle flanked by intrinsically disordered N- and C-terminal tails. Split-intein-mediated segmental NMR-active isotope-enrichment allowed unambiguous demonstration of modular and malleable "beads-on-a-string" concatemeric behaviour. Concatemers form fibres upon manual drawing with silk-like morphology and mechanical properties, alongside secondary structuring and orientation consistent with native AcSp1 fibres. AcSp1 structural stability varies locally, with the fifth helix denaturing most readily. The structural transition of aciniform spidroin from a mostly α-helical dope to a mixed α-helix/β-sheet-containing fibre can be directly related to spidroin architecture and stability.


  • Organizational Affiliation

    Department of Biochemistry &Molecular Biology, Dalhousie University, Halifax, NS, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aciniform spidroin 1199Argiope trifasciataMutation(s): 0 
UniProt
Find proteins for Q64K55 (Argiope trifasciata)
Explore Q64K55 
Go to UniProtKB:  Q64K55
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ64K55
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-07-08
    Type: Initial release
  • Version 1.1: 2023-06-14
    Changes: Data collection, Database references, Other