1khw
From Proteopedia
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Crystal Structure of Rabbit Hemorrhagic Disease Virus RNA-dependent RNA polymerase complexed with Mn2+
Overview
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-A resolution. The overall structure resembles a "right hand," as, seen before in other polymerases, including the RdRPs 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, approximately 8 degrees. Metal ions bind at different positions in the two, conformations and suggest how structural changes may be important to, enzymatic function in RdRPs. 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.
About this Structure
1KHW is a Single protein structure of sequence from Rabbit hemorrhagic disease virus with MN as ligand. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Full crystallographic information is available from OCA.
Reference
Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase., Ng KK, Cherney MM, Vazquez AL, Machin A, Alonso JM, Parra F, James MN, J Biol Chem. 2002 Jan 11;277(2):1381-7. Epub 2001 Oct 24. PMID:11677245
Page seeded by OCA on Tue Nov 20 19:15:15 2007
