5J37

Crystal structure of 60-mer BFDV Capsid Protein in complex with single stranded DNA

5J37 の概要

• エントリーDOI: 10.2210/pdb5j37/pdb
• 関連するPDBエントリー: 5J09 5J36
• 分子名称: Beak and feather disease virus capsid protein, single stranded DNA, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: bfdv virus capsid jelly roll, viral protein, virus-dna complex, virus/dna
• 由来する生物種: Beak and feather disease virus (BFDV); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 197190.66

構造登録者

Sarker, S.,Raidal, S.,Aragao, D.,Forwood, J.K. (登録日: 2016-03-30, 公開日: 2016-05-04, 最終更新日: 2023-10-25)

主引用文献

Sarker, S.,Terron, M.C.,Khandokar, Y.,Aragao, D.,Hardy, J.M.,Radjainia, M.,Jimenez-Zaragoza, M.,de Pablo, P.J.,Coulibaly, F.,Luque, D.,Raidal, S.R.,Forwood, J.K.
Structural insights into the assembly and regulation of distinct viral capsid complexes.
Nat Commun, 7:13014-13014, 2016

PubMed Abstract: The assembly and regulation of viral capsid proteins into highly ordered macromolecular complexes is essential for viral replication. Here, we utilize crystal structures of the capsid protein from the smallest and simplest known viruses capable of autonomously replicating in animal cells, circoviruses, to establish structural and mechanistic insights into capsid morphogenesis and regulation. The beak and feather disease virus, like many circoviruses, encode only two genes: a capsid protein and a replication initiation protein. The capsid protein forms distinct macromolecular assemblies during replication and here we elucidate these structures at high resolution, showing that these complexes reverse the exposure of the N-terminal arginine rich domain responsible for DNA binding and nuclear localization. We show that assembly of these complexes is regulated by single-stranded DNA (ssDNA), and provide a structural basis of capsid assembly around single-stranded DNA, highlighting novel binding interfaces distinct from the highly positively charged N-terminal ARM domain.

PubMed: 27698405
DOI: 10.1038/ncomms13014

実験手法

X-RAY DIFFRACTION (2.3 Å)