2p4v | pdb_00002p4v
Crystal structure of the transcript cleavage factor, GreB at 2.6A resolution
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Overview
Bacterial Gre transcript cleavage factors stimulate the intrinsic, endonucleolytic activity of RNA polymerase (RNAP) to rescue stalled, transcription complexes. They bind to RNAP and extend their coiled-coil, (CC) domains to the catalytic centre through the secondary channel. Three, existing models for the Gre-RNAP complex postulate congruent mechanisms of, Gre-assisted catalysis, while offering conflicting views of the Gre-RNAP, interactions. Here, we report the GreB structure of Escherichia coli. The, GreB monomers form a triangle with the tip of the amino-terminal CC of one, molecule trapped within the hydrophobic cavity of the carboxy-terminal, domain of a second molecule. This arrangement suggests an analogous model, for recruitment to RNAP. Indeed, the beta'-subunit CC located at the rim, of the secondary channel has conserved hydrophobic residues at its tip. We, show that substitutions of these residues and those in the GreB C-terminal, domain cavity confer defects in GreB activity and binding to RNAP, and, present a plausible model for the RNAP-GreB complex.
About this Structure
2P4V is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The carboxy-terminal coiled-coil of the RNA polymerase beta'-subunit is the main binding site for Gre factors., Vassylyeva MN, Svetlov V, Dearborn AD, Klyuyev S, Artsimovitch I, Vassylyev DG, EMBO Rep. 2007 Nov;8(11):1038-43. Epub 2007 Oct 5. PMID:17917675
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