3C6E

Crystal structure of the precursor membrane protein- envelope protein heterodimer from the dengue 2 virus at neutral pH

Summary for 3C6E

• Entry DOI: 10.2210/pdb3c6e/pdb
• Related: 3C5X
• Descriptor: Envelope protein E, prM, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: beta barrel, prm-e protein complex structure, helicase, hydrolase, nucleotide-binding, rna replication, transmembrane, viral protein
• Biological source: Dengue virus 2 Thailand/16681/84; More
• Total number of polymer chains: 2
• Total formula weight: 60863.40

Authors

Li, L. (deposition date: 2008-02-04, release date: 2008-04-08, Last modification date: 2023-08-30)

Primary citation

Li, L.,Lok, S.M.,Yu, I.M.,Zhang, Y.,Kuhn, R.J.,Chen, J.,Rossmann, M.G.
The flavivirus precursor membrane-envelope protein complex: structure and maturation.
Science, 319:1830-1834, 2008

PubMed Abstract: Many viruses go through a maturation step in the final stages of assembly before being transmitted to another host. The maturation process of flaviviruses is directed by the proteolytic cleavage of the precursor membrane protein (prM), turning inert virus into infectious particles. We have determined the 2.2 angstrom resolution crystal structure of a recombinant protein in which the dengue virus prM is linked to the envelope glycoprotein E. The structure represents the prM-E heterodimer and fits well into the cryo-electron microscopy density of immature virus at neutral pH. The pr peptide beta-barrel structure covers the fusion loop in E, preventing fusion with host cell membranes. The structure provides a basis for identifying the stages of its pH-directed conformational metamorphosis during maturation, ending with release of pr when budding from the host.

PubMed: 18369147
DOI: 10.1126/science.1153263

Experimental method

X-RAY DIFFRACTION (2.6 Å)