1QDP

SOLUTION STRUCTURE OF ROBUSTOXIN, THE LETHAL NEUROTOXIN FROM THE FUNNEL WEB SPIDER ATRAX ROBUSTUS, NMR, 20 STRUCTURES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 20 
  • Selection Criteria: TOTAL, NOE & DIHEDRAL ENERGY 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus.

Pallaghy, P.K.Alewood, D.Alewood, P.F.Norton, R.S.

(1997) FEBS Lett 419: 191-196

  • DOI: https://doi.org/10.1016/s0014-5793(97)01452-x
  • Primary Citation of Related Structures:  
    1QDP

  • PubMed Abstract: 

    The solution structure of robustoxin, the lethal neurotoxin from the Sydney funnel-web spider Atrax robustus, has been determined from 2D 1H NMR data. Robustoxin is a polypeptide of 42 residues cross-linked by four disulphide bonds, the connectivities of which were determined from NMR data and trial structure calculations to be 1-15, 8-20, 14-31 and 16-42 (a 1-4/2-6/3-7/5-8 pattern). The structure consists of a small three-stranded, anti-parallel beta-sheet and a series of interlocking gamma-turns at the C-terminus. It also contains a cystine knot, thus placing it in the inhibitor cystine knot motif family of structures, which includes the omega-conotoxins and a number of plant and animal toxins and protease inhibitors. Robustoxin contains three distinct charged patches on its surface, and an extended loop that includes several aromatic and non-polar residues. Both of these structural features may play a role in its binding to the voltage-gated sodium channel.


  • Organizational Affiliation

    Biomolecular Research Institute, Parkville, Vic., Australia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ROBUSTOXIN42Atrax robustusMutation(s): 0 
UniProt
Find proteins for P01478 (Atrax robustus)
Explore P01478 
Go to UniProtKB:  P01478
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01478
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 20 
  • Selection Criteria: TOTAL, NOE & DIHEDRAL ENERGY 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-01-14
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Database references, Derived calculations, Other