Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KHW

Crystal Structure of Rabbit Hemorrhagic Disease Virus RNA-dependent RNA polymerase complexed with Mn2+

Summary for 1KHW
Entry DOI10.2210/pdb1khw/pdb
Related1KHV
DescriptorRNA-DIRECTED RNA POLYMERASE, MANGANESE (II) ION (3 entities in total)
Functional Keywordsrna-dependent rna polymerase, transferase
Biological sourceRabbit hemorrhagic disease virus
Total number of polymer chains2
Total formula weight115882.50
Authors
Ng, K.K.,Cherney, M.M.,Vazquez, A.L.,Machin, A.,Alonso, J.M.,Parra, F.,James, M.N. (deposition date: 2001-12-01, release date: 2002-01-16, Last modification date: 2024-11-06)
Primary citationNg, K.K.,Cherney, M.M.,Vazquez, A.L.,Machin, A.,Alonso, J.M.,Parra, F.,James, M.N.
Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase.
J.Biol.Chem., 277:1381-1387, 2002
Cited by
PubMed Abstract: 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.
PubMed: 11677245
DOI: 10.1074/jbc.M109261200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon