6CO8

Structure of Zika virus at a resolution of 3.1 Angstrom

Summary for 6CO8

• Entry DOI: 10.2210/pdb6co8/pdb
• EMDB information: 7543
• Descriptor: E protein, M protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: zika, flavivirus, virus
• Biological source: Zika virus ZIKV/H. sapiens/FrenchPolynesia/10087PF/2013 (isolate ZIKV/Human/French Polynesia/10087PF/2013); More
• Total number of polymer chains: 6
• Total formula weight: 190096.01

Authors

Sevvana, M.,Long, F.,Miller, A.J.,Klose, T.,Buda, G.,Sun, L.,Kuhn, R.J.,Rossmann, M.R. (deposition date: 2018-03-12, release date: 2018-07-04, Last modification date: 2024-10-23)

Primary citation

Sevvana, M.,Long, F.,Miller, A.S.,Klose, T.,Buda, G.,Sun, L.,Kuhn, R.J.,Rossmann, M.G.
Refinement and Analysis of the Mature Zika Virus Cryo-EM Structure at 3.1 angstrom Resolution.
Structure, 26:1169-, 2018

PubMed Abstract: Among the several arthropod-borne human flaviviral diseases, the recent outbreak of Zika virus (ZIKV) has caused devastating birth defects and neurological disorders, challenging the world with another major public health concern. We report here the refined structure of the mature ZIKV at a resolution of 3.1 Å as determined by cryo-electron microscopic single-particle reconstruction. The improvement in the resolution, compared with previous enveloped virus structures, was the result of optimized virus preparation methods and data processing techniques. The glycoprotein interactions and surface properties of ZIKV were compared with other mosquito-borne flavivirus structures. The largest structural differences and sequence variations occur at the glycosylation loop associated with receptor binding. Probable drug binding pockets were identified on the viral surface. These results also provide a structural basis for the design of vaccines against ZIKV.

PubMed: 29958768
DOI: 10.1016/j.str.2018.05.006

Experimental method

ELECTRON MICROSCOPY (3.1 Å)