3F6N

Crystal structure of the virion-associated protein P3 from Caulimovirus

3F6N の概要

• エントリーDOI: 10.2210/pdb3f6n/pdb
• 分子名称: Virion-associated protein (2 entities in total)
• 機能のキーワード: coiled-coil, viral protein, tetramer, dna-binding, virion, dna-binding protein
• 由来する生物種: Cauliflower mosaic virus (STRAIN STRASBOURG) (CaMV)
• 細胞内の位置: Virion: P03551
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56672.62

構造登録者

Hoh, F.,Uzest, M.,Blanc, S.,Dumas, C. (登録日: 2008-11-06, 公開日: 2009-11-24, 最終更新日: 2024-10-30)

主引用文献

Hoh, F.,Uzest, M.,Drucker, M.,Plisson-Chastang, C.,Bron, P.,Blanc, S.,Dumas, C.
Structural insights into the molecular mechanisms of cauliflower mosaic virus transmission by its insect vector.
J.Virol., 84:4706-4713, 2010

PubMed Abstract: Cauliflower mosaic virus (CaMV) is transmitted from plant to plant through a seemingly simple interaction with insect vectors. This process involves an aphid receptor and two viral proteins, P2 and P3. P2 binds to both the aphid receptor and P3, itself tightly associated with the virus particle, with the ensemble forming a transmissible viral complex. Here, we describe the conformations of both unliganded CaMV P3 protein and its virion-associated form. X-ray crystallography revealed that the N-terminal domain of unliganded P3 is a tetrameric parallel coiled coil with a unique organization showing two successive four-stranded subdomains with opposite supercoiling handedness stabilized by a ring of interchain disulfide bridges. A structural model of virus-liganded P3 proteins, folding as an antiparallel coiled-coil network coating the virus surface, was derived from molecular modeling. Our results highlight the structural and biological versatility of this coiled-coil structure and provide new insights into the molecular mechanisms involved in CaMV acquisition and transmission by the insect vector.

PubMed: 20181714
DOI: 10.1128/JVI.02662-09

実験手法

X-RAY DIFFRACTION (3.1 Å)