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3J0F

Sindbis virion

Summary for 3J0F
Entry DOI10.2210/pdb3j0f/pdb
EMDB information5251
DescriptorCapsid protein, E1 envelope glycoprotein, E2 envelope glycoprotein (3 entities in total)
Functional Keywordsalphavirus, virus assembly, glycoprotein, virus
Biological sourceSindbis virus (SINV)
More
Cellular locationCapsid protein: Virion (By similarity). p62: Virion membrane; Single-pass type I membrane protein (By similarity). E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein (By similarity). E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein (By similarity). 6K protein: Host cell membrane; Multi-pass membrane protein (By similarity): P03316 P03316 P03316
Total number of polymer chains12
Total formula weight495237.71
Authors
Tang, J.,Jose, J.,Zhang, W.,Chipman, P.,Kuhn, R.J.,Baker, T.S. (deposition date: 2011-07-08, release date: 2011-10-12, Last modification date: 2024-02-21)
Primary citationTang, J.,Jose, J.,Chipman, P.,Zhang, W.,Kuhn, R.J.,Baker, T.S.
Molecular Links between the E2 Envelope Glycoprotein and Nucleocapsid Core in Sindbis Virus.
J.Mol.Biol., 414:442-459, 2011
Cited by
PubMed Abstract: A three-dimensional reconstruction of Sindbis virus at 7.0 Å resolution presented here provides a detailed view of the virion structure and includes structural evidence for key interactions that occur between the capsid protein (CP) and transmembrane (TM) glycoproteins E1 and E2. Based on crystal structures of component proteins and homology modeling, we constructed a nearly complete, pseudo-atomic model of the virus. Notably, this includes identification of the 33-residue cytoplasmic domain of E2 (cdE2), which follows a path from the E2 TM helix to the CP where it enters and exits the CP hydrophobic pocket and then folds back to contact the viral membrane. Modeling analysis identified three major contact regions between cdE2 and CP, and the roles of specific residues were probed by molecular genetics. This identified R393 and E395 of cdE2 and Y162 and K252 of CP as critical for virus assembly. The N-termini of the CPs form a contiguous network that interconnects 12 pentameric and 30 hexameric CP capsomers. A single glycoprotein spike cross-links three neighboring CP capsomers as might occur during initiation of virus budding.
PubMed: 22001018
DOI: 10.1016/j.jmb.2011.09.045
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7 Å)
Structure validation

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数据于2025-06-25公开中

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