6yi2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:10, 19 June 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==UvrD helicase RNA polymerase interactions are governed by UvrDs carboxy terminal Tudor domain.==
==UvrD helicase RNA polymerase interactions are governed by UvrDs carboxy terminal Tudor domain.==
-
<StructureSection load='6yi2' size='340' side='right'caption='[[6yi2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+
<StructureSection load='6yi2' size='340' side='right'caption='[[6yi2]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6yi2]] 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=6YI2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YI2 FirstGlance]. <br>
+
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YI2 FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uvrD, ACU57_06555 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6yi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yi2 OCA], [https://pdbe.org/6yi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yi2 RCSB], [https://www.ebi.ac.uk/pdbsum/6yi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yi2 ProSAT]</span></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=6yi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yi2 OCA], [http://pdbe.org/6yi2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yi2 RCSB], [http://www.ebi.ac.uk/pdbsum/6yi2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yi2 ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
 
-
== 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.
 
-
UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.,Kawale AA, Burmann BM Commun Biol. 2020 Oct 23;3(1):607. doi: 10.1038/s42003-020-01332-2. PMID:33097771<ref>PMID:33097771</ref>
+
==See Also==
-
 
+
*[[Helicase 3D structures|Helicase 3D structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6yi2" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bacillus coli migula 1895]]
 
-
[[Category: DNA helicase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Burmann, B B]]
+
[[Category: Burmann BB]]
-
[[Category: Kawale, A A]]
+
[[Category: Kawale AA]]
-
[[Category: Dna-repair]]
+
-
[[Category: Protein binding]]
+
-
[[Category: Tcr]]
+
-
[[Category: Tudor]]
+
-
[[Category: Uvrd]]
+

Current revision

UvrD helicase RNA polymerase interactions are governed by UvrDs carboxy terminal Tudor domain.

PDB ID 6yi2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools