2MS0
Solution NMR structure pf tRNApro:MLV-Nucleocapsid (1:2) Complex
Summary for 2MS0
| Entry DOI | 10.2210/pdb2ms0/pdb |
| Related | 2MQT 2MQV 2MS1 |
| NMR Information | BMRB: 25100 |
| Descriptor | Nucleocapsid protein p10, tRNApro, ZINC ION (3 entities in total) |
| Functional Keywords | viral protein-rna complex, retroviral primer annealing, nucleocapsid chaperone, primer binding site, viral protein/rna |
| Biological source | Murine leukemia virus More |
| Cellular location | Gag-Pol polyprotein: Host cell membrane ; Lipid-anchor . Matrix protein p15: Virion . Capsid protein p30: Virion . Nucleocapsid protein p10: Virion : P03355 |
| Total number of polymer chains | 3 |
| Total formula weight | 35829.88 |
| Authors | D'Souza, V.,Yildiz, Z. (deposition date: 2014-07-19, release date: 2014-09-17, Last modification date: 2024-05-01) |
| Primary citation | Miller, S.B.,Yildiz, F.Z.,Lo, J.A.,Wang, B.,D'Souza, V.M. A structure-based mechanism for tRNA and retroviral RNA remodelling during primer annealing. Nature, 515:591-595, 2014 Cited by PubMed Abstract: 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. PubMed: 25209668DOI: 10.1038/nature13709 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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