2P4V
Crystal structure of the transcript cleavage factor, GreB at 2.6A resolution
Summary for 2P4V
| Entry DOI | 10.2210/pdb2p4v/pdb |
| Related | 1GRJ 2ETN 2EUL 2F23 |
| Descriptor | Transcription elongation factor greB (2 entities in total) |
| Functional Keywords | transcription, transcript cleavage, gre-factors, rna polymerase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 6 |
| Total formula weight | 111438.65 |
| Authors | Vassylyeva, M.N.,Svetlov, V.,Dearborn, A.D.,Klyuyev, S.,Artsimovitch, I.,Vassylyev, D.G. (deposition date: 2007-03-13, release date: 2008-01-22, Last modification date: 2024-02-21) |
| Primary citation | Vassylyeva, M.N.,Svetlov, V.,Dearborn, A.D.,Klyuyev, S.,Artsimovitch, I.,Vassylyev, D.G. The carboxy-terminal coiled-coil of the RNA polymerase beta'-subunit is the main binding site for Gre factors. Embo Rep., 8:1038-1043, 2007 Cited by PubMed Abstract: 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. PubMed: 17917675DOI: 10.1038/sj.embor.7401079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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