3mlq

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

spinqualitylabelsall models 3mlq, resolution 2.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3mlq is a 8 chain structure with sequence from Atcc 25104 and Thet2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Gene: rpoB (ATCC 25104), mfd, TT_C0533 (THET2) Activity: DNA-directed RNA polymerase, with EC number 2.7.7.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q72KB4_THET2] Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.[HAMAP-Rule:MF_00969] Publication Abstract from PubMed 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 beta-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 beta-subunit. We determined the 2.9-A resolution X-ray crystal structure of the RNAP interacting domain of TRCF complexed with the RNAP-beta1 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. Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction.,Westblade LF, Campbell EA, Pukhrambam C, Padovan JC, Nickels BE, Lamour V, Darst SA Nucleic Acids Res. 2010 Aug 11. PMID:20702425 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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