3MLQ

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

3MLQ の概要

• エントリーDOI: 10.2210/pdb3mlq/pdb
• 分子名称: DNA-directed RNA polymerase subunit beta, Transcription-repair coupling factor, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: tudor, transferase-transcription complex, transferase/transcription
• 由来する生物種: Thermus aquaticus; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 116428.02

構造登録者

Darst, S.A.,Westblade, L.F.,Campbell, E.A. (登録日: 2010-04-18, 公開日: 2010-10-13, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.91 Å)