4AGK

Crystal structure of capsid protein (110-267) from Aura virus

4AGK の概要

• エントリーDOI: 10.2210/pdb4agk/pdb
• 関連するPDBエントリー: 4AGJ
• 分子名称: CAPSID PROTEIN (2 entities in total)
• 機能のキーワード: hydrolase, viral protein
• 由来する生物種: AURA VIRUS
• 細胞内の位置: Capsid protein: Virion (By similarity). p62: Virion membrane; Single-pass type I membrane protein (By similarity). E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein (By similarity). E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein (By similarity). 6K protein: Host cell membrane; Multi-pass membrane protein (By similarity): Q86925
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17008.25

構造登録者

Aggarwal, M.,Kumar, P.,Tomar, S. (登録日: 2012-01-30, 公開日: 2012-12-26, 最終更新日: 2023-12-20)

主引用文献

Aggarwal, M.,Tapas, S.,Preeti,Siwach, A.,Kumar, P.,Kuhn, R.J.,Tomar, S.
Crystal Structure of Aura Virus Capsid Protease and its Complex with Dioxane: New Insights Into Capsid-Glycoprotein Molecular Contacts
Plos One, 7:51288-, 2012

PubMed Abstract: The nucleocapsid core interaction with endodomains of glycoproteins plays a critical role in the alphavirus life cycle that is essential to virus budding. Recent cryo-electron microscopy (cryo-EM) studies provide structural insights into key interactions between capsid protein (CP) and trans-membrane glycoproteins E1 and E2. CP possesses a chymotrypsin-like fold with a hydrophobic pocket at the surface responsible for interaction with glycoproteins. In the present study, crystal structures of the protease domain of CP from Aura virus and its complex with dioxane were determined at 1.81 and 1.98 Å resolution respectively. Due to the absence of crystal structures, homology models of E1 and E2 from Aura virus were generated. The crystal structure of CP and structural models of E1 and E2 were fitted into the cryo-EM density map of Venezuelan equine encephalitis virus (VEEV) for detailed analysis of CP-glycoprotein interactions. Structural analysis revealed that the E2 endodomain consists of a helix-loop-helix motif where the loop region fits into the hydrophobic pocket of CP. Our studies suggest that Cys397, Cys418 and Tyr401 residues of E2 are involved in stabilizing the structure of E2 endodomain. Density map fitting analysis revealed that Pro405, a conserved E2 residue is present in the loop region of the E2 endodomain helix-loop-helix structure and makes intermolecular hydrophobic contacts with the capsid. In the Aura virus capsid protease (AVCP)-dioxane complex structure, dioxane occupies the hydrophobic pocket on CP and structurally mimics the hydrophobic pyrollidine ring of Pro405 in the loop region of E2.

PubMed: 23251484
DOI: 10.1371/JOURNAL.PONE.0051288

実験手法

X-RAY DIFFRACTION (1.81 Å)