1LJ2
Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization
Summary for 1LJ2
| Entry DOI | 10.2210/pdb1lj2/pdb |
| Descriptor | NONSTRUCTURAL RNA-BINDING PROTEIN 34, eukaryotic protein synthesis initiation factor, GOLD ION, ... (4 entities in total) |
| Functional Keywords | nsp3; homodimer; eif4g; rotavirus; translation; mrna; closed loop; coiled coil, viral protein- translation complex, viral protein/ translation |
| Biological source | Simian rotavirus A/SA11 More |
| Total number of polymer chains | 4 |
| Total formula weight | 32683.00 |
| Authors | Groft, C.M.,Burley, S.K. (deposition date: 2002-04-18, release date: 2002-07-05, Last modification date: 2024-02-14) |
| Primary citation | Groft, C.M.,Burley, S.K. Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization. Mol.Cell, 9:1273-1283, 2002 Cited by PubMed Abstract: Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely alpha-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure. PubMed: 12086624DOI: 10.1016/S1097-2765(02)00555-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
Download full validation report
