2HG0

Structure of the West Nile Virus envelope glycoprotein

Summary for 2HG0

• Entry DOI: 10.2210/pdb2hg0/pdb
• Related: 1OAN 1OKE 1SVB 1TG8 1UZG
• Descriptor: Envelope glycoprotein, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: virus/viral protein, viral protein
• Biological source: West Nile virus
• Total number of polymer chains: 1
• Total formula weight: 44815.64

Authors

Nybakken, G.E.,Nelson, C.A.,Chen, B.R.,Diamond, M.S.,Fremont, D.H. (deposition date: 2006-06-26, release date: 2006-11-07, Last modification date: 2024-10-30)

Primary citation

Nybakken, G.E.,Nelson, C.A.,Chen, B.R.,Diamond, M.S.,Fremont, D.H.
Crystal structure of the West Nile virus envelope glycoprotein.
J.Virol., 80:11467-11474, 2006

PubMed Abstract: The envelope glycoprotein (E) of West Nile virus (WNV) undergoes a conformational rearrangement triggered by low pH that results in a class II fusion event required for viral entry. Herein we present the 3.0-A crystal structure of the ectodomain of WNV E, which reveals insights into the flavivirus life cycle. We found that WNV E adopts a three-domain architecture that is shared by the E proteins from dengue and tick-borne encephalitis viruses and forms a rod-shaped configuration similar to that observed in immature flavivirus particles. Interestingly, the single N-linked glycosylation site on WNV E is displaced by a novel alpha-helix, which could potentially alter lectin-mediated attachment. The localization of histidines within the hinge regions of E implicates these residues in pH-induced conformational transitions. Most strikingly, the WNV E ectodomain crystallized as a monomer, in contrast to other flavivirus E proteins, which have crystallized as antiparallel dimers. WNV E assembles in a crystalline lattice of perpendicular molecules, with the fusion loop of one E protein buried in a hydrophobic pocket at the DI-DIII interface of another. Dimeric E proteins pack their fusion loops into analogous pockets at the dimer interface. We speculate that E proteins could pivot around the fusion loop-pocket junction, allowing virion conformational transitions while minimizing fusion loop exposure.

PubMed: 16987985
DOI: 10.1128/JVI.01125-06

Experimental method

X-RAY DIFFRACTION (3 Å)