Conservation of the 3B contact surface at the base of the palm of 3Dpol among picornaviruses [Dataset]

Abstract

(A) Structure-based sequence alignment of the picornavirus 3Dpol residues located the base of the palm that would participate in interactions with 3B, (B) Structural superimposition of the two quasi-equivalent 3B1 binding sites in FMDV 3Dpol. The polymerase residues and the bound 3B1 regions are shown in sticks, coloured as in Fig 1, but with molecule I shown in semi-transparent. (C) The 3B binding site in EV71 3Dpol, as seen in the X-ray structure of the EV71 3Dpol -3B complex [11] (PDB:4IKA). (D-G) Structural comparisons of the putative 3B binding region in 3Dpol of other representative picornaviruses whose structure is known: the enteroviruses PV [5] (PDB: 1RA7; light blue) (D) and HRV1B [7] (PDB: 1XR6; salmon) (E), the cardiovirus EMCV [14] (PDB: 4NYZ; cyan) (F), and the kobusvirus porcine aichi virus [13](PDB: 6R1I; green).