3MLQ

Crystal structure of the Thermus thermophilus transcription-repair coupling factor RNA polymerase interacting domain with the Thermus aquaticus RNA polymerase beta1 domain

Summary for 3MLQ

• Entry DOI: 10.2210/pdb3mlq/pdb
• Descriptor: DNA-directed RNA polymerase subunit beta, Transcription-repair coupling factor, PHOSPHATE ION (3 entities in total)
• Functional Keywords: tudor, transferase-transcription complex, transferase/transcription
• Biological source: Thermus aquaticus; More
• Total number of polymer chains: 8
• Total formula weight: 116428.02

Authors

Darst, S.A.,Westblade, L.F.,Campbell, E.A. (deposition date: 2010-04-18, release date: 2010-10-13, Last modification date: 2024-04-03)

Primary citation

Westblade, L.F.,Campbell, E.A.,Pukhrambam, C.,Padovan, J.C.,Nickels, B.E.,Lamour, V.,Darst, S.A.
Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction.
Nucleic Acids Res., 38:8357-8369, 2010

PubMed Abstract: The transcription-repair coupling factor (TRCF, the product of the mfd gene) is a widely conserved bacterial protein that mediates transcription-coupled DNA repair. TRCF uses its ATP-dependent DNA translocase activity to remove transcription complexes stalled at sites of DNA damage, and stimulates repair by recruiting components of the nucleotide excision repair pathway to the site. A protein/protein interaction between TRCF and the β-subunit of RNA polymerase (RNAP) is essential for TRCF function. CarD (also called CdnL), an essential regulator of rRNA transcription in Mycobacterium tuberculosis, shares a homologous RNAP interacting domain with TRCF and also interacts with the RNAP β-subunit. We determined the 2.9-Å resolution X-ray crystal structure of the RNAP interacting domain of TRCF complexed with the RNAP-β1 domain, which harbors the TRCF interaction determinants. The structure reveals details of the TRCF/RNAP protein/protein interface, providing a basis for the design and interpretation of experiments probing TRCF, and by homology CarD, function and interactions with the RNAP.

PubMed: 20702425
DOI: 10.1093/nar/gkq692

Experimental method

X-RAY DIFFRACTION (2.91 Å)