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1uon
From Proteopedia
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REOVIRUS POLYMERASE LAMBDA-3 LOCALIZED BY ELECTRON CRYOMICROSCOPY OF VIRIONS AT 7.6-A RESOLUTION
Overview
Reovirus is an icosahedral, double-stranded (ds) RNA virus that uses viral, polymerases packaged within the viral core to transcribe its ten distinct, plus-strand RNAs. To localize these polymerases, the structure of the, reovirion was refined to a resolution of 7.6 A by cryo-electron microscopy, (cryo-EM) and three-dimensional (3D) image reconstruction. X-ray crystal, models of reovirus proteins, including polymerase lambda 3, were then, fitted into the density map. Each copy of lambda 3 was found anchored to, the inner surface of the icosahedral core shell, making major contacts, with three molecules of shell protein lambda 1 and overlapping, but not, centering on, a five-fold axis. The overlap explains why only one copy of, lambda 3 is bound per vertex. lambda 3 is furthermore oriented with its, transcript exit channel facing a small channel through the lambda 1 shell, suggesting how the nascent RNA is passed into the large external cavity of, the pentameric capping enzyme complex formed by protein lambda 2.
About this Structure
1UON is a Protein complex structure of sequences from Reovirus sp. with MN and CH1 as ligands. Full crystallographic information is available from OCA.
Reference
Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A., Zhang X, Walker SB, Chipman PR, Nibert ML, Baker TS, Nat Struct Biol. 2003 Dec;10(12):1011-8. Epub 2003 Nov 9. PMID:14608373
Page seeded by OCA on Wed Nov 21 04:16:44 2007
Categories: Protein complex | Reovirus sp. | Baker, T.S. | Chipman, P.R. | Nibert, M.L. | Walker, S.B. | Zhang, X. | CH1 | MN | Core protein | Cryoem | Polymerase | Reovirus
