2f8e
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Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with uridylylated VPg protein
OverviewOverview
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.
About this StructureAbout this Structure
2F8E is a Single protein structure of sequence from Foot-and-mouth disease virus c with , and as ligands. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Full crystallographic information is available from OCA.
ReferenceReference
The structure of a protein primer-polymerase complex in the initiation of genome replication., Ferrer-Orta C, Arias A, Agudo R, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N, EMBO J. 2006 Feb 22;25(4):880-8. Epub 2006 Feb 2. PMID:16456546
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