Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB–DNA complexes
UvrB has a central role in the highly conserved UvrABC pathway functioning not only as a damage recognition element but also as an essential component of the lesion tracking machinery. While it has been recently confirmed that the tracking assembly comprises a UvrA2B2 heterotetramer, the configurati...
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| Format: | Online |
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Oxford University Press
2012
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3458569/ |
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pubmed-34585692012-09-27 Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB–DNA complexes Webster, Matthew P. J. Jukes, Rachael Zamfir, Vlad S. Kay, Christopher W. M. Bagnéris, Claire Barrett, Tracey Structural Biology UvrB has a central role in the highly conserved UvrABC pathway functioning not only as a damage recognition element but also as an essential component of the lesion tracking machinery. While it has been recently confirmed that the tracking assembly comprises a UvrA2B2 heterotetramer, the configurations of the damage engagement and UvrB–DNA handover complexes remain obscure. Here, we present the first crystal structure of a UvrB dimer whose biological significance has been verified using both chemical cross-linking and electron paramagnetic resonance spectroscopy. We demonstrate that this dimeric species stably associates with UvrA and forms a UvrA2B2–DNA complex. Our studies also illustrate how signals are transduced between the ATP and DNA binding sites to generate the helicase activity pivotal to handover and formation of the UvrB2–DNA complex, providing key insights into the configurations of these important repair intermediates. Oxford University Press 2012-09 2012-06-30 /pmc/articles/PMC3458569/ /pubmed/22753105 http://dx.doi.org/10.1093/nar/gks633 Text en © The Author(s) 2012. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Webster, Matthew P. J. Jukes, Rachael Zamfir, Vlad S. Kay, Christopher W. M. Bagnéris, Claire Barrett, Tracey |
| spellingShingle |
Webster, Matthew P. J. Jukes, Rachael Zamfir, Vlad S. Kay, Christopher W. M. Bagnéris, Claire Barrett, Tracey Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB–DNA complexes |
| author_facet |
Webster, Matthew P. J. Jukes, Rachael Zamfir, Vlad S. Kay, Christopher W. M. Bagnéris, Claire Barrett, Tracey |
| author_sort |
Webster, Matthew P. J. |
| title |
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB–DNA complexes |
| title_short |
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB–DNA complexes |
| title_full |
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB–DNA complexes |
| title_fullStr |
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB–DNA complexes |
| title_full_unstemmed |
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB–DNA complexes |
| title_sort |
crystal structure of the uvrb dimer: insights into the nature and functioning of the uvrab damage engagement and uvrb–dna complexes |
| description |
UvrB has a central role in the highly conserved UvrABC pathway functioning not only as a damage recognition element but also as an essential component of the lesion tracking machinery. While it has been recently confirmed that the tracking assembly comprises a UvrA2B2 heterotetramer, the configurations of the damage engagement and UvrB–DNA handover complexes remain obscure. Here, we present the first crystal structure of a UvrB dimer whose biological significance has been verified using both chemical cross-linking and electron paramagnetic resonance spectroscopy. We demonstrate that this dimeric species stably associates with UvrA and forms a UvrA2B2–DNA complex. Our studies also illustrate how signals are transduced between the ATP and DNA binding sites to generate the helicase activity pivotal to handover and formation of the UvrB2–DNA complex, providing key insights into the configurations of these important repair intermediates. |
| publisher |
Oxford University Press |
| publishDate |
2012 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3458569/ |
| _version_ |
1611911954195021824 |