6yhz

<StructureSection load='6yhz' size='340' side='right'caption='[[6yhz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[6yhz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YHZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YHZ FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mfd, ELT49_18965 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yhz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yhz OCA], [http://pdbe.org/6yhz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yhz RCSB], [http://www.ebi.ac.uk/pdbsum/6yhz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yhz ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/A0A5F0Q0Z8_ECOLX A0A5F0Q0Z8_ECOLX]] 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]

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== Publication Abstract from PubMed ==

All living organisms have to cope with the constant threat of genome damage by UV light and other toxic reagents. To maintain the integrity of their genomes, organisms developed a variety of DNA repair pathways. One of these, the Transcription Coupled DNA-Repair (TCR) pathway, is triggered by stalled RNA Polymerase (RNAP) complexes at DNA damage sites on actively transcribed genes. A recently elucidated bacterial TCR pathway employs the UvrD helicase pulling back stalled RNAP complexes from the damage, stimulating recruitment of the DNA-repair machinery. However, structural and functional aspects of UvrD's interaction with RNA Polymerase remain elusive. Here we used advanced solution NMR spectroscopy to investigate UvrD's role within the TCR, identifying that the carboxy-terminal region of the UvrD helicase facilitates RNAP interactions by adopting a Tudor-domain like fold. Subsequently, we functionally analyzed this domain, identifying it as a crucial component for the UvrD-RNAP interaction besides having nucleic-acid affinity.

 

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== References ==

[[Category: Bacillus coli migula 1895]]

[[Category: Burmann, B B]]

[[Category: Kawale, A A]]

[[Category: Tudor]]