聚合酶
核糖核酸
RNA依赖性RNA聚合酶
生物
RNA聚合酶
病毒学
逆转录酶
病毒
DNA聚合酶
鼠疫病毒
DNA
分子生物学
遗传学
基因
丙型肝炎病毒
黄病毒科
作者
Kyung Hyun Choi,Andreas Gallei,Paul Becher,Michael G. Rossmann
出处
期刊:Structure
[Elsevier]
日期:2006-07-01
卷期号:14 (7): 1107-1113
被引量:61
标识
DOI:10.1016/j.str.2006.05.020
摘要
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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