6G67

Crystal structure of a parallel eight-helix coiled coil CC-Type2-II


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.77 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.205 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Maintaining and breaking symmetry in homomeric coiled-coil assemblies.

Rhys, G.G.Wood, C.W.Lang, E.J.M.Mulholland, A.J.Brady, R.L.Thomson, A.R.Woolfson, D.N.

(2018) Nat Commun 9: 4132-4132

  • DOI: https://doi.org/10.1038/s41467-018-06391-y
  • Primary Citation of Related Structures:  
    6G65, 6G66, 6G67, 6G68, 6G69, 6G6A, 6G6B, 6G6C, 6G6D, 6G6E, 6G6F, 6G6G, 6G6H

  • PubMed Abstract: 

    In coiled-coil (CC) protein structures α-helices wrap around one another to form rope-like assemblies. Most natural and designed CCs have two-four helices and cyclic (C n ) or dihedral (D n ) symmetry. Increasingly, CCs with five or more helices are being reported. A subset of these higher-order CCs is of interest as they have accessible central channels that can be functionalised; they are α-helical barrels. These extended cavities are surprising given the drive to maximise buried hydrophobic surfaces during protein folding and assembly in water. Here, we show that α-helical barrels can be maintained by the strategic placement of β-branched aliphatic residues lining the lumen. Otherwise, the structures collapse or adjust to give more-complex multi-helix assemblies without C n or D n symmetry. Nonetheless, the structural hallmark of CCs-namely, knobs-into-holes packing of side chains between helices-is maintained leading to classes of CCs hitherto unobserved in nature or accessed by design.


  • Organizational Affiliation

    School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. Guto.Rhys@bristol.ac.uk.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CC-Type2-II
A, B
32synthetic constructMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GOL
Query on GOL

Download Ideal Coordinates CCD File 
C [auth B]GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.77 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.205 
  • Space Group: I 4 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 48.11α = 90
b = 48.11β = 90
c = 126.969γ = 90
Software Package:
Software NamePurpose
iMOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Engineering and Physical Sciences Research CouncilUnited KingdomEP/G036764/1
European Research CouncilUnited Kingdom340764

Revision History  (Full details and data files)

  • Version 1.0: 2018-10-17
    Type: Initial release