TY - JOUR
T1 - The Structure of Bovine Viral Diarrhea Virus RNA-Dependent RNA Polymerase and Its Amino-Terminal Domain
AU - Choi, Kyung H.
AU - Gallei, Andreas
AU - Becher, Paul
AU - Rossmann, Michael G.
N1 - Funding Information:
We thank Tim Schmidt for his assistance with data collection. We thank the MacCHESS (Cornell High Energy Synchrotron Source) and APS (Advanced Photon Source) beamline staffs for help in data collection. We thank Sharon Wilder and Cheryl Towell for help in the preparation of the manuscript. This work was supported by a Purdue University Trask Fund to K.H.C. and a National Institutes of Health Program Project Grant to M.G.R. (AI 57153).
PY - 2006/7
Y1 - 2006/7
N2 - Viral RNA-dependent RNA polymerases (RdRp) differ from DNA-dependent RNA polymerases, DNA-dependent DNA polymerases, and reverse transcriptases in that RdRps contain "fingertips" consisting of several polypeptide strands in the fingers domain interacting with the thumb domain. The crystal structure of bovine viral diarrhea virus (BVDV) RdRp containing an Asn438 duplication shows that the "N-terminal domain," which occurs only in pestiviruses such as BVDV, interacts with the polymerase component of the same polypeptide chain. This contrasts with the domain swapping observed in the previously determined structure of the BVDV NADL strain RdRp. By comparison with the NADL structure and through the use of biochemical data, it is possible that the N-terminal domain, in conjunction with the fingertips, is required to bind and assist the translocation of the RNA template. The partial disorder of the loop containing the additional Asn438 residue may explain the low replication rate of the recombinant compared with the wild-type virus.
AB - Viral RNA-dependent RNA polymerases (RdRp) differ from DNA-dependent RNA polymerases, DNA-dependent DNA polymerases, and reverse transcriptases in that RdRps contain "fingertips" consisting of several polypeptide strands in the fingers domain interacting with the thumb domain. The crystal structure of bovine viral diarrhea virus (BVDV) RdRp containing an Asn438 duplication shows that the "N-terminal domain," which occurs only in pestiviruses such as BVDV, interacts with the polymerase component of the same polypeptide chain. This contrasts with the domain swapping observed in the previously determined structure of the BVDV NADL strain RdRp. By comparison with the NADL structure and through the use of biochemical data, it is possible that the N-terminal domain, in conjunction with the fingertips, is required to bind and assist the translocation of the RNA template. The partial disorder of the loop containing the additional Asn438 residue may explain the low replication rate of the recombinant compared with the wild-type virus.
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U2 - 10.1016/j.str.2006.05.020
DO - 10.1016/j.str.2006.05.020
M3 - Article
C2 - 16843892
AN - SCOPUS:33745832659
SN - 0969-2126
VL - 14
SP - 1107
EP - 1113
JO - Structure
JF - Structure
IS - 7
ER -