2YQ2

Structure of BVDV1 envelope glycoprotein E2, pH8

2YQ2 の概要

• エントリーDOI: 10.2210/pdb2yq2/pdb
• 関連するPDBエントリー: 2YQ3
• 分子名称: BVDV1 E2, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: viral protein, pestivirus, virus fusion
• 由来する生物種: BOVINE VIRAL DIARRHEA VIRUS 1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77644.33

構造登録者

El Omari, K.,Iourin, O.,Harlos, K.,Grimes, J.M.,Stuart, D.I. (登録日: 2012-11-04, 公開日: 2013-01-16, 最終更新日: 2024-10-23)

主引用文献

El Omari, K.,Iourin, O.,Harlos, K.,Grimes, J.M.,Stuart, D.I.
Structure of a Pestivirus Envelope Glycoprotein E2 Clarifies its Role in Cell Entry.
Cell Rep., 3:30-, 2013

PubMed Abstract: Enveloped viruses have developed various adroit mechanisms to invade their host cells. This process requires one or more viral envelope glycoprotein to achieve cell attachment and membrane fusion. Members of the Flaviviridae such as flaviviruses possess only one envelope glycoprotein, E, whereas pestiviruses and hepacivirus encode two glycoproteins, E1 and E2. Although E2 is involved in cell attachment, it has been unclear which protein is responsible for membrane fusion. We report the crystal structures of the homodimeric glycoprotein E2 from the pestivirus bovine viral diarrhea virus 1 (BVDV1) at both neutral and low pH. Unexpectedly, BVDV1 E2 does not have a class II fusion protein fold, and at low pH the N-terminal domain is disordered, similarly to the intermediate postfusion state of E2 from sindbis virus, an alphavirus. Our results suggest that the pestivirus and possibly the hepacivirus fusion machinery are unlike any previously observed.

PubMed: 23273918
DOI: 10.1016/J.CELREP.2012.12.001

実験手法

X-RAY DIFFRACTION (2.58 Å)