1Z8Y

Mapping the E2 Glycoprotein of Alphaviruses


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 9.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses.

Mukhopadhyay, S.Zhang, W.Gabler, S.Chipman, P.R.Strauss, E.G.Strauss, J.H.Baker, T.S.Kuhn, R.J.Rossmann, M.G.

(2006) Structure 14: 63-73

  • DOI: https://doi.org/10.1016/j.str.2005.07.025
  • Primary Citation of Related Structures:  
    1Z8Y

  • PubMed Abstract: 

    The 9 A resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and E2 glycoproteins in the formation of a heterodimer, on the difference in conformation of the two types of trimeric spikes, on the interaction between the transmembrane helices of the E1 and E2 proteins, and on the conformational changes that occur when fusing with a host cell. The positions of various markers on the E2 protein established the approximate topology of the E2 structure. The largest conformational differences between the icosahedral surface spikes at icosahedral 3-fold and quasi-3-fold positions are associated with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are shown to rotate by about 180 degrees and to move away from the center of the spikes during fusion.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA. sumukhop@indiana.edu


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Spike glycoprotein E1
A, C, E, G
290Sindbis virusMutation(s): 0 
UniProt
Find proteins for P03316 (Sindbis virus)
Explore P03316 
Go to UniProtKB:  P03316
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03316
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Spike glycoprotein E1
B, D, F, H
89Sindbis virusMutation(s): 0 
UniProt
Find proteins for P03316 (Sindbis virus)
Explore P03316 
Go to UniProtKB:  P03316
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03316
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Spike glycoprotein E1
I, K, M, O
31Sindbis virusMutation(s): 0 
UniProt
Find proteins for P03316 (Sindbis virus)
Explore P03316 
Go to UniProtKB:  P03316
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03316
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Spike glycoprotein E2
J, L, N, P
36Sindbis virusMutation(s): 0 
UniProt
Find proteins for P03316 (Sindbis virus)
Explore P03316 
Go to UniProtKB:  P03316
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03316
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein C
Q, R, S, T
151Sindbis virusMutation(s): 0 
EC: 3.4.21
UniProt
Find proteins for P03316 (Sindbis virus)
Explore P03316 
Go to UniProtKB:  P03316
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03316
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 9.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONPURDUE PROGRAMS

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-02-07
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-07-18
    Changes: Data collection
  • Version 1.4: 2019-11-06
    Changes: Data collection, Other