2MS1: Solution NMR structure of tRNApro:MLV Nucleocapsid Protein (1:1) Complex

To prime reverse transcription, retroviruses require annealing of a transfer RNA molecule to the U5 primer binding site (U5-PBS) region of the viral genome. The residues essential for primer annealing are initially locked in intramolecular interactions; hence, annealing requires the chaperone activity of the retroviral nucleocapsid (NC) protein to facilitate structural rearrangements. Here we show that, unlike classical chaperones, the Moloney murine leukaemia virus NC uses a unique mechanism for remodelling: it specifically targets multiple structured regions in both the U5-PBS and tRNA(Pro) primer that otherwise sequester residues necessary for annealing. This high-specificity and high-affinity binding by NC consequently liberates these sequestered residues--which are exactly complementary--for intermolecular interactions. Furthermore, NC utilizes a step-wise, entropy-driven mechanism to trigger both residue-specific destabilization and residue-specific release. Our structures of NC bound to U5-PBS and tRNA(Pro) reveal the structure-based mechanism for retroviral primer annealing and provide insights as to how ATP-independent chaperones can target specific RNAs amidst the cellular milieu of non-target RNAs.
PDB ID: 2MS1Download
MMDB ID: 122970
PDB Deposition Date: 2014/7/19
Updated in MMDB: 2014/10
Experimental Method:
solution nmr
Source Organism:
Murine leukemia virus
Similar Structures:
Biological Unit for 2MS1: dimeric; determined by author and by software (PISA)
Molecular Components in 2MS1
Label Count Molecule
Protein (1 molecule)
Nucleocapsid Protein P10(Gene symbol: gag-pol)
Molecule annotation
Nucleotide(1 molecule)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB