2D7S
Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with VPg protein
Summary for 2D7S
| Entry DOI | 10.2210/pdb2d7s/pdb |
| Related | 1U09 1WNE |
| Descriptor | RNA-dependent RNA polymerase, VPg1 protein (2 entities in total) |
| Functional Keywords | foot and mouth disease virus, rna-dependent rna polymerase, 3d polymerase, vpg, protein-primer, transferase |
| Biological source | Foot-and-mouth disease virus More |
| Total number of polymer chains | 2 |
| Total formula weight | 55876.53 |
| Authors | Ferrer-Orta, C.,Arias, A.,Perez-Luque, R.,Escarmis, C.,Domingo, E.,Verdaguer, N. (deposition date: 2005-11-29, release date: 2006-03-28, Last modification date: 2023-10-25) |
| Primary citation | Ferrer-Orta, C.,Arias, A.,Agudo, R.,Perez-Luque, R.,Escarmis, C.,Domingo, E.,Verdaguer, N. The structure of a protein primer-polymerase complex in the initiation of genome replication Embo J., 25:880-888, 2006 Cited by PubMed Abstract: Picornavirus RNA replication is initiated by the covalent attachment of a UMP molecule to the hydroxyl group of a tyrosine in the terminal protein VPg. This reaction is carried out by the viral RNA-dependent RNA polymerase (3D). Here, we report the X-ray structure of two complexes between foot-and-mouth disease virus 3D, VPg1, the substrate UTP and divalent cations, in the absence and in the presence of an oligoadenylate of 10 residues. In both complexes, VPg fits the RNA binding cleft of the polymerase and projects the key residue Tyr3 into the active site of 3D. This is achieved by multiple interactions with residues of motif F and helix alpha8 of the fingers domain and helix alpha13 of the thumb domain of the polymerase. The complex obtained in the presence of the oligoadenylate showed the product of the VPg uridylylation (VPg-UMP). Two metal ions and the catalytic aspartic acids of the polymerase active site, together with the basic residues of motif F, have been identified as participating in the priming reaction. PubMed: 16456546DOI: 10.1038/sj.emboj.7600971 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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