1MWH

REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG

Summary for 1MWH

• Entry DOI: 10.2210/pdb1mwh/pdb
• Related: 1MUK
• Descriptor: MINOR CORE PROTEIN LAMBDA 3, MANGANESE (II) ION, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE, ... (4 entities in total)
• Functional Keywords: polymerase, polymerase-cap analog complex, right hand configuration, viral protein
• Biological source: Reovirus sp.
• Cellular location: Virion (Potential): P17378
• Total number of polymer chains: 1
• Total formula weight: 143282.17

Authors

Tao, Y.,Farsetta, D.L.,Nibert, M.L.,Harrison, S.C. (deposition date: 2002-09-29, release date: 2002-12-18, Last modification date: 2024-02-14)

Primary citation

Tao, Y.,Farsetta, D.L.,Nibert, M.L.,Harrison, S.C.
RNA Synthesis in a Cage-Structural Studies of Reovirus Polymerase lambda3
Cell(Cambridge,Mass.), 111:733-745, 2002

PubMed Abstract: The reovirus polymerase and those of other dsRNA viruses function within the confines of a protein capsid to transcribe the tightly packed dsRNA genome segments. The crystal structure of the reovirus polymerase, lambda3, determined at 2.5 A resolution, shows a fingers-palm-thumb core, similar to those of other viral polymerases, surrounded by major N- and C-terminal elaborations, which create a cage-like structure, with four channels leading to the catalytic site. This "caged" polymerase has allowed us to visualize the results of several rounds of RNA polymerization directly in the crystals. A 5' cap binding site on the surface of lambda3 suggests a template retention mechanism by which attachment of the 5' end of the plus-sense strand facilitates insertion of the 3' end of the minus-sense strand into the template channel.

PubMed: 12464184
DOI: 10.1016/S0092-8674(02)01110-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)