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X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain

Genome maintenance is an essential process in all cells. In prokaryotes, the RadD protein is important for survival under conditions that include DNA-damaging radiation. Precisely how RadD participates in genome maintenance remains unclear. Here we present a high-resolution X-ray crystal structure o...

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Autores principales: Osorio Garcia, Miguel A., Satyshur, Kenneth A., Cox, Michael M., Keck, James L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9049331/
https://www.ncbi.nlm.nih.gov/pubmed/35482735
http://dx.doi.org/10.1371/journal.pone.0266031
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author Osorio Garcia, Miguel A.
Satyshur, Kenneth A.
Cox, Michael M.
Keck, James L.
author_facet Osorio Garcia, Miguel A.
Satyshur, Kenneth A.
Cox, Michael M.
Keck, James L.
author_sort Osorio Garcia, Miguel A.
collection PubMed
description Genome maintenance is an essential process in all cells. In prokaryotes, the RadD protein is important for survival under conditions that include DNA-damaging radiation. Precisely how RadD participates in genome maintenance remains unclear. Here we present a high-resolution X-ray crystal structure of ADP-bound Escherichia coli RadD, revealing a zinc-ribbon element that was not modelled in a previous RadD crystal structure. Insights into the mode of nucleotide binding and additional structure refinement afforded by the new RadD model will help to drive investigations into the activity of RadD as a genome stability and repair factor.
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spelling pubmed-90493312022-04-29 X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain Osorio Garcia, Miguel A. Satyshur, Kenneth A. Cox, Michael M. Keck, James L. PLoS One Research Article Genome maintenance is an essential process in all cells. In prokaryotes, the RadD protein is important for survival under conditions that include DNA-damaging radiation. Precisely how RadD participates in genome maintenance remains unclear. Here we present a high-resolution X-ray crystal structure of ADP-bound Escherichia coli RadD, revealing a zinc-ribbon element that was not modelled in a previous RadD crystal structure. Insights into the mode of nucleotide binding and additional structure refinement afforded by the new RadD model will help to drive investigations into the activity of RadD as a genome stability and repair factor. Public Library of Science 2022-04-28 /pmc/articles/PMC9049331/ /pubmed/35482735 http://dx.doi.org/10.1371/journal.pone.0266031 Text en © 2022 Osorio Garcia et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Osorio Garcia, Miguel A.
Satyshur, Kenneth A.
Cox, Michael M.
Keck, James L.
X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain
title X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain
title_full X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain
title_fullStr X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain
title_full_unstemmed X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain
title_short X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain
title_sort x-ray crystal structure of the escherichia coli radd dna repair protein bound to adp reveals a novel zinc ribbon domain
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9049331/
https://www.ncbi.nlm.nih.gov/pubmed/35482735
http://dx.doi.org/10.1371/journal.pone.0266031
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