Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1U6P

NMR Structure of the MLV encapsidation signal bound to the Nucleocapsid protein

Summary for 1U6P
Entry DOI10.2210/pdb1u6p/pdb
Related1S9S
Descriptor101-MER, Gag polyprotein, ZINC ION (3 entities in total)
Functional Keywordsmlv, a-minor k-turn, stem loop, bulge, g-u mismatch, g-a mismatch, u-u mismatch, a-c mismatch, zinc finger, nc, viral protein-rna complex, viral protein/rna
Biological sourceMoloney murine leukemia virus
More
Cellular locationGag polyprotein: Virion (By similarity). Matrix protein p15: Virion (Potential). Capsid protein p30: Virion (Potential). Nucleocapsid protein p10: Virion (Potential): P03332
Total number of polymer chains2
Total formula weight39147.10
Authors
D'Souza, V.,Summers, M.F. (deposition date: 2004-07-30, release date: 2004-11-02, Last modification date: 2024-05-01)
Primary citationD'Souza, V.,Summers, M.F.
Structural basis for packaging the dimeric genome of Moloney murine leukaemia virus
Nature, 431:586-590, 2004
Cited by
PubMed Abstract: All retroviruses specifically package two copies of their genomes during virus assembly, a requirement for strand-transfer-mediated recombination during reverse transcription. Genomic RNA exists in virions as dimers, and the overlap of RNA elements that promote dimerization and encapsidation suggests that these processes may be coupled. Both processes are mediated by the nucleocapsid domain (NC) of the retroviral Gag polyprotein. Here we show that dimerization-induced register shifts in base pairing within the Psi-RNA packaging signal of Moloney murine leukaemia virus (MoMuLV) expose conserved UCUG elements that bind NC with high affinity (dissociation constant = 75 +/- 12 nM). These elements are base-paired and do not bind NC in the monomeric RNA. The structure of the NC complex with a 101-nucleotide 'core encapsidation' segment of the MoMuLV Psi site reveals a network of interactions that promote sequence- and structure-specific binding by NC's single CCHC zinc knuckle. Our findings support a structural RNA switch mechanism for genome encapsidation, in which protein binding sites are sequestered by base pairing in the monomeric RNA and become exposed upon dimerization to promote packaging of a diploid genome.
PubMed: 15457265
DOI: 10.1038/nature02944
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon