期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 277, 期 2, 页码 1381-1387出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109261200
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资金
- NCRR NIH HHS [RR07707] Funding Source: Medline
The structure of the RNA-dependent RNA polymerase (RdRP) from the rabbit hemorrhagic disease virus has been determined by x-ray crystallography to a 2.5-Angstrom resolution. The overall structure resembles a right hand, as seen before in other polymerases, including the RdRP`s of polio virus and hepatitis C virus. Two copies of the polymerase are present in the asymmetric unit of the crystal, revealing active and inactive conformations within the same crystal form. The fingers and palm domains form a relatively rigid unit, but the thumb domain can adopt either closed or open conformations differing by a rigid body rotation of similar to8 degrees. Metal ions bind at different positions in the two conformations and suggest how structural changes may be important to enzymatic function in RdRP`s. Comparisons between the structures of the alternate conformational states of rabbit hemorrhagic disease virus RdRP and the structures of RdRPs from hepatitis C virus and polio virus suggest novel structure-function relationships in this medically important class of enzymes.
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