Transcription-repair coupling factor
From Proteopedia
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+ | <StructureSection load='2eyq' size='350' side='right' scene='2eyq/Asymmunit/2' caption=''> | ||
[[Image:2eyq.png|left|200px|thumb|Crystal Structure of Transcription-repair coupling factor [[2eyq]]]] | [[Image:2eyq.png|left|200px|thumb|Crystal Structure of Transcription-repair coupling factor [[2eyq]]]] | ||
- | <StructureSection load='2eyq' size='350' side='right' scene='2eyq/Asymmunit/2' caption='2eyq asymmetric unit, resolution 3.20Å. <br> Click <scene name='2eyq/Biolunit/1'>here</scene> to display biological molecule'> | ||
'''Transcription-repair coupling factor (TRCF)''' enables the coupling of these processes in bacteria and humans. The TRCF has ATPase activity. <scene name='2eyq/Asymmunit/2'>The crystallographic asymmetric unit of the solved structure contains 2 monomers of Mfd (residues 2-1147 of 1151 for one molecule and 5-1147 of the other), five HEPES molecules, and the sulfate ions.</scene> | '''Transcription-repair coupling factor (TRCF)''' enables the coupling of these processes in bacteria and humans. The TRCF has ATPase activity. <scene name='2eyq/Asymmunit/2'>The crystallographic asymmetric unit of the solved structure contains 2 monomers of Mfd (residues 2-1147 of 1151 for one molecule and 5-1147 of the other), five HEPES molecules, and the sulfate ions.</scene> |
Revision as of 10:34, 7 June 2012
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Reference
- Deaconescu AM, Chambers AL, Smith AJ, Nickels BE, Hochschild A, Savery NJ, Darst SA. Structural basis for bacterial transcription-coupled DNA repair. Cell. 2006 Feb 10;124(3):507-20. PMID:16469698 doi:10.1016/j.cell.2005.11.045
Created with the participation of Wayne Decatur
Proteopedia Page Contributors and Editors (what is this?)
Karsten Theis, Michal Harel, Alexander Berchansky, Wayne Decatur