1TG8

The structure of Dengue virus E glycoprotein

Summary for 1TG8

• Entry DOI: 10.2210/pdb1tg8/pdb
• Related: 1TGE 1THD
• Descriptor: envelope glycoprotein, 2-acetamido-2-deoxy-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: flavivirus e conformation, viral protein
• Biological source: Dengue virus 2
• Cellular location: Envelope protein E: Virion membrane; Multi- pass membrane protein (By similarity). Non-structural protein 1: Secreted. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P27914
• Total number of polymer chains: 1
• Total formula weight: 44305.81

Authors

Zhang, Y.,Zhang, W.,Ogata, S.,Clements, D.,Strauss, J.H.,Baker, T.S.,Rossmann, M.G. (deposition date: 2004-05-28, release date: 2004-09-28, Last modification date: 2024-11-13)

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

X-RAY DIFFRACTION (2.61 Å)