4GV5

X-ray structure of crotamine, a cell-penetrating peptide from the Brazilian snake Crotalus durissus terrificus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.225 
  • R-Value Work: 0.167 
  • R-Value Observed: 0.170 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of the polypeptide crotamine from the Brazilian rattlesnake Crotalus durissus terrificus.

Coronado, M.A.Gabdulkhakov, A.Georgieva, D.Sankaran, B.Murakami, M.T.Arni, R.K.Betzel, C.

(2013) Acta Crystallogr D Biol Crystallogr 69: 1958-1964

  • DOI: https://doi.org/10.1107/S0907444913018003
  • Primary Citation of Related Structures:  
    4GV5

  • PubMed Abstract: 

    The crystal structure of the myotoxic, cell-penetrating, basic polypeptide crotamine isolated from the venom of Crotalus durissus terrificus has been determined by single-wavelength anomalous dispersion techniques and refined at 1.7 Å resolution. The structure reveals distinct cationic and hydrophobic surface regions that are located on opposite sides of the molecule. This surface-charge distribution indicates its possible mode of interaction with negatively charged phospholipids and other molecular targets to account for its diverse pharmacological activities. Although the sequence identity between crotamine and human β-defensins is low, the three-dimensional structures of these functionally related peptides are similar. Since crotamine is a leading member of a large family of myotoxic peptides, its structure will provide a basis for the design of novel cell-penetrating molecules.


  • Organizational Affiliation

    Multi User Center for Biomolecular Innovation, Department of Physics, São Paulo State University, UNESP/IBILCE, C. Postal 136, 15054-000 São José do Rio Preto-SP, Brazil.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Crotamine Ile-19
A, B, C
42Crotalus durissus terrificusMutation(s): 0 
UniProt
Find proteins for Q9PWF3 (Crotalus durissus terrificus)
Explore Q9PWF3 
Go to UniProtKB:  Q9PWF3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9PWF3
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

Download Ideal Coordinates CCD File 
H [auth B],
I [auth B],
K [auth C]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
GOL
Query on GOL

Download Ideal Coordinates CCD File 
F [auth A],
G [auth A],
M [auth C],
N [auth C]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
SCN
Query on SCN

Download Ideal Coordinates CCD File 
D [auth A],
E [auth A],
J [auth B],
L [auth C]
THIOCYANATE ION
C N S
ZMZDMBWJUHKJPS-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.225 
  • R-Value Work: 0.167 
  • R-Value Observed: 0.170 
  • Space Group: I 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 66.922α = 90
b = 74.33β = 90
c = 80.199γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
AutoSolphasing
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-09-04
    Type: Initial release
  • Version 1.1: 2013-10-23
    Changes: Database references
  • Version 1.2: 2018-03-07
    Changes: Data collection
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Derived calculations