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Structure of a hexameric form of RadA recombinase from Methanococcus voltae
Archaeal RadA proteins are close homologues of eukaryal Rad51 and DMC1 proteins and are remote homologues of bacterial RecA proteins. For the repair of double-stranded breaks in DNA, these recombinases promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2012
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374503/ https://www.ncbi.nlm.nih.gov/pubmed/22691778 http://dx.doi.org/10.1107/S1744309112010226 |
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author | Du, Liqin Luo, Yu |
author_facet | Du, Liqin Luo, Yu |
author_sort | Du, Liqin |
collection | PubMed |
description | Archaeal RadA proteins are close homologues of eukaryal Rad51 and DMC1 proteins and are remote homologues of bacterial RecA proteins. For the repair of double-stranded breaks in DNA, these recombinases promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. This DNA-repair function also plays a key role in the resistance of cancer cells to chemotherapy and radiotherapy and in the resistance of bacterial cells to antibiotics. A hexameric form of a truncated Methanococcus voltae RadA protein devoid of its small N-terminal domain has been crystallized. The RadA hexamers further assemble into two-ringed assemblies. Similar assemblies can be observed in the crystals of Pyrococcus furiosus RadA and Homo sapiens DMC1. In all of these two-ringed assemblies the DNA-interacting L1 region of each protomer points inward towards the centre, creating a highly positively charged locus. The electrostatic characteristics of the central channels can be utilized in the design of novel recombinase inhibitors. |
format | Online Article Text |
id | pubmed-3374503 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-33745032012-06-20 Structure of a hexameric form of RadA recombinase from Methanococcus voltae Du, Liqin Luo, Yu Acta Crystallogr Sect F Struct Biol Cryst Commun Structural Communications Archaeal RadA proteins are close homologues of eukaryal Rad51 and DMC1 proteins and are remote homologues of bacterial RecA proteins. For the repair of double-stranded breaks in DNA, these recombinases promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. This DNA-repair function also plays a key role in the resistance of cancer cells to chemotherapy and radiotherapy and in the resistance of bacterial cells to antibiotics. A hexameric form of a truncated Methanococcus voltae RadA protein devoid of its small N-terminal domain has been crystallized. The RadA hexamers further assemble into two-ringed assemblies. Similar assemblies can be observed in the crystals of Pyrococcus furiosus RadA and Homo sapiens DMC1. In all of these two-ringed assemblies the DNA-interacting L1 region of each protomer points inward towards the centre, creating a highly positively charged locus. The electrostatic characteristics of the central channels can be utilized in the design of novel recombinase inhibitors. International Union of Crystallography 2012-04-20 /pmc/articles/PMC3374503/ /pubmed/22691778 http://dx.doi.org/10.1107/S1744309112010226 Text en © Du & Luo 2012 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Structural Communications Du, Liqin Luo, Yu Structure of a hexameric form of RadA recombinase from Methanococcus voltae |
title | Structure of a hexameric form of RadA recombinase from Methanococcus voltae
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title_full | Structure of a hexameric form of RadA recombinase from Methanococcus voltae
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title_fullStr | Structure of a hexameric form of RadA recombinase from Methanococcus voltae
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title_full_unstemmed | Structure of a hexameric form of RadA recombinase from Methanococcus voltae
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title_short | Structure of a hexameric form of RadA recombinase from Methanococcus voltae
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title_sort | structure of a hexameric form of rada recombinase from methanococcus voltae |
topic | Structural Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374503/ https://www.ncbi.nlm.nih.gov/pubmed/22691778 http://dx.doi.org/10.1107/S1744309112010226 |
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