1Z8Y

Mapping the E2 Glycoprotein of Alphaviruses

Summary for 1Z8Y

• Entry DOI: 10.2210/pdb1z8y/pdb
• Related: 1LD4
• EMDB information: 1121
• Descriptor: Spike glycoprotein E1, Spike glycoprotein E2, Capsid protein C, ... (5 entities in total)
• Functional Keywords: icosahedral enveloped virus, icosahedral virus, virus
• Biological source: Sindbis virus; More
• Total number of polymer chains: 20
• Total formula weight: 258383.24

Authors

Mukhopadhyay, S.,Zhang, W.,Gabler, S.,Chipman, P.R.,Strauss, E.G.,Strauss, J.H.,Baker, T.S.,Kuhn, R.J.,Rossmann, M.G. (deposition date: 2005-03-31, release date: 2006-02-07, Last modification date: 2024-11-13)

Primary citation

Mukhopadhyay, S.,Zhang, W.,Gabler, S.,Chipman, P.R.,Strauss, E.G.,Strauss, J.H.,Baker, T.S.,Kuhn, R.J.,Rossmann, M.G.
Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses.
Structure, 14:63-73, 2006

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.

PubMed: 16407066
DOI: 10.1016/j.str.2005.07.025

Experimental method

ELECTRON MICROSCOPY (9 Å)