1UON

REOVIRUS POLYMERASE LAMBDA-3 LOCALIZED BY ELECTRON CRYOMICROSCOPY OF VIRIONS AT 7.6-A RESOLUTION

Summary for 1UON

• Entry DOI: 10.2210/pdb1uon/pdb
• Related: 1MUK 1MWH 1N1H 1N35 1N38
• Descriptor: MINOR CORE PROTEIN LAMBDA 3, 5'-R(*GP*GP*GP*GP*GP*)-3', 5'-R(*UP*AP*GP*CP*CP*CP*CP*CP*)-3', ... (6 entities in total)
• Functional Keywords: polymerase, reovirus, cryoem, core protein
• Biological source: REOVIRUS; More
• Total number of polymer chains: 3
• Total formula weight: 148077.74

Authors

Zhang, X.,Walker, S.B.,Chipman, P.R.,Nibert, M.L.,Baker, T.S. (deposition date: 2003-09-21, release date: 2003-11-13, Last modification date: 2024-05-08)

Primary citation

Zhang, X.,Walker, S.B.,Chipman, P.R.,Nibert, M.L.,Baker, T.S.
Reovirus Polymerase Lambda3 Localized by Cryo-Electron Microscopy of Virions at a Resolution of 7.6 A
Nat.Struct.Biol., 10:1011-, 2003

PubMed Abstract: 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.

PubMed: 14608373
DOI: 10.1038/NSB1009

Experimental method

ELECTRON MICROSCOPY (7.6 Å)