1n1h

From Proteopedia

---

Revision as of 19:45, 20 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1n1h, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Initiation complex of polymerase lambda3 from reovirus

Overview

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.

About this Structure

1N1H is a Single protein structure of sequence from Mammalian orthoreovirus 3 with MN, G7M, GDP, CH1 and GH3 as ligands. Full crystallographic information is available from OCA.

Reference

RNA synthesis in a cage--structural studies of reovirus polymerase lambda3., Tao Y, Farsetta DL, Nibert ML, Harrison SC, Cell. 2002 Nov 27;111(5):733-45. PMID:12464184

Page seeded by OCA on Tue Nov 20 21:52:22 2007