1THD

COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION

Summary for 1THD

• Entry DOI: 10.2210/pdb1thd/pdb
• Related: 1P58 1TG8
• Descriptor: Major envelope protein E (1 entity in total)
• Functional Keywords: flavivirus, flaviviridae, dengue virus, glycoprotein e, cryo-em, icosahedral virus, virus
• Biological source: Dengue virus 2 Puerto Rico/PR159-S1/1969
• Total number of polymer chains: 3
• Total formula weight: 131590.19

Authors

Zhang, Y.,Zhang, W.,Ogata, S.,Clements, D.,Strauss, J.H.,Baker, T.S.,Kuhn, R.J.,Rossmann, M.G. (deposition date: 2004-06-01, release date: 2004-09-28, Last modification date: 2024-02-14)

Primary citation

Zhang, Y.,Zhang, W.,Ogata, S.,Clements, D.,Strauss, J.H.,Baker, T.S.,Kuhn, R.J.,Rossmann, M.G.
Conformational changes of the flavivirus e glycoprotein
Structure, 12:1607-1618, 2004

PubMed Abstract: Dengue virus, a member of the Flaviviridae family, has a surface composed of 180 copies each of the envelope (E) glycoprotein and the membrane (M) protein. The crystal structure of an N-terminal fragment of E has been determined and compared with a previously described structure. The primary difference between these structures is a 10 degrees rotation about a hinge relating the fusion domain DII to domains DI and DIII. These two rigid body components were used for independent fitting of E into the cryo-electron microscopy maps of both immature and mature dengue viruses. The fitted E structures in these two particles showed a difference of 27 degrees between the two components. Comparison of the E structure in its postfusion state with that in the immature and mature virions shows a rotation approximately around the same hinge. Flexibility of E is apparently a functional requirement for assembly and infection of flaviviruses.

PubMed: 15341726
DOI: 10.1016/j.str.2004.06.019

Experimental method

ELECTRON MICROSCOPY (9.5 Å)