3J27

CryoEM structure of Dengue virus

Summary for 3J27

• Entry DOI: 10.2210/pdb3j27/pdb
• Related: 3J2P
• EMDB information: 5499 5520
• Descriptor: Envelope protein E, Small envelope protein M, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: flavivirus, fusion protein, protein complex, membrane, chaperone, virus
• Biological source: Dengue virus 2 (DENV-2); More
• Total number of polymer chains: 6
• Total formula weight: 189806.97

Authors

Zhang, X.,Ge, P.,Yu, X.,Brannan, J.M.,Bi, G.,Zhang, Q.,Schein, S.,Zhou, Z.H. (deposition date: 2012-09-26, release date: 2012-12-19, Last modification date: 2024-11-20)

Primary citation

Zhang, X.,Ge, P.,Yu, X.,Brannan, J.M.,Bi, G.,Zhang, Q.,Schein, S.,Zhou, Z.H.
Cryo-EM structure of the mature dengue virus at 3.5-A resolution.
Nat.Struct.Mol.Biol., 20:105-110, 2012

PubMed Abstract: Regulated by pH, membrane-anchored proteins E and M function during dengue virus maturation and membrane fusion. Our atomic model of the whole virion from cryo-electron microscopy at 3.5-Å resolution reveals that in the mature virus at neutral extracellular pH, the N-terminal 20-amino-acid segment of M (involving three pH-sensing histidines) latches and thereby prevents spring-loaded E fusion protein from prematurely exposing its fusion peptide. This M latch is fastened at an earlier stage, during maturation at acidic pH in the trans-Golgi network. At a later stage, to initiate infection in response to acidic pH in the late endosome, M releases the latch and exposes the fusion peptide. Thus, M serves as a multistep chaperone of E to control the conformational changes accompanying maturation and infection. These pH-sensitive interactions could serve as targets for drug discovery.

PubMed: 23241927
DOI: 10.1038/nsmb.2463

Experimental method

ELECTRON MICROSCOPY (3.6 Å)