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| [[Image:2p4v.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2p4v.png|left|200px]] |
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| {{STRUCTURE_2p4v| PDB=2p4v | SCENE= }} | | {{STRUCTURE_2p4v| PDB=2p4v | SCENE= }} |
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| '''Crystal structure of the transcript cleavage factor, GreB at 2.6A resolution'''
| | ===Crystal structure of the transcript cleavage factor, GreB at 2.6A resolution=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17917675}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17917675 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17917675}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Transcript cleavage]] | | [[Category: Transcript cleavage]] |
| [[Category: Transcription]] | | [[Category: Transcription]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:21:59 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:57:03 2008'' |
