5J37

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

Summary for 5J37

• Entry DOI: 10.2210/pdb5j37/pdb
• Related: 5J09 5J36
• Descriptor: Beak and feather disease virus capsid protein, single stranded DNA, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: bfdv virus capsid jelly roll, viral protein, virus-dna complex, virus/dna
• Biological source: Beak and feather disease virus (BFDV); More
• Total number of polymer chains: 10
• Total formula weight: 197190.66

Authors

Sarker, S.,Raidal, S.,Aragao, D.,Forwood, J.K. (deposition date: 2016-03-30, release date: 2016-05-04, Last modification date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)