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Crystal structure of the NurA–dAMP–Mn(2+) complex

Generation of the 3′ overhang is a critical event during homologous recombination (HR) repair of DNA double strand breaks. A 5′–3′ nuclease, NurA, plays an important role in generating 3′ single-stranded DNA during archaeal HR, together with Mre11–Rad50 and HerA. We have determined the crystal struc...

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Detalles Bibliográficos
Autores principales: Chae, Jina, Kim, Young Chang, Cho, Yunje
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3300031/
https://www.ncbi.nlm.nih.gov/pubmed/22064858
http://dx.doi.org/10.1093/nar/gkr999
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author Chae, Jina
Kim, Young Chang
Cho, Yunje
author_facet Chae, Jina
Kim, Young Chang
Cho, Yunje
author_sort Chae, Jina
collection PubMed
description Generation of the 3′ overhang is a critical event during homologous recombination (HR) repair of DNA double strand breaks. A 5′–3′ nuclease, NurA, plays an important role in generating 3′ single-stranded DNA during archaeal HR, together with Mre11–Rad50 and HerA. We have determined the crystal structures of apo- and dAMP-Mn(2)(+)-bound NurA from Pyrococcus furiousus (Pf NurA) to provide the basis for its cleavage mechanism. Pf NurA forms a pyramid-shaped dimer containing a large central channel on one side, which becomes narrower towards the peak of the pyramid. The structure contains a PIWI domain with high similarity to argonaute, endoV nuclease and RNase H. The two active sites, each of which contains Mn(2)(+) ion(s) and dAMP, are at the corners of the elliptical channel near the flat face of the dimer. The 3′ OH group of the ribose ring is directed toward the channel entrance, explaining the 5′–3′ nuclease activity of Pf NurA. We provide a DNA binding and cleavage model for Pf NurA.
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spelling pubmed-33000312012-03-13 Crystal structure of the NurA–dAMP–Mn(2+) complex Chae, Jina Kim, Young Chang Cho, Yunje Nucleic Acids Res Structural Biology Generation of the 3′ overhang is a critical event during homologous recombination (HR) repair of DNA double strand breaks. A 5′–3′ nuclease, NurA, plays an important role in generating 3′ single-stranded DNA during archaeal HR, together with Mre11–Rad50 and HerA. We have determined the crystal structures of apo- and dAMP-Mn(2)(+)-bound NurA from Pyrococcus furiousus (Pf NurA) to provide the basis for its cleavage mechanism. Pf NurA forms a pyramid-shaped dimer containing a large central channel on one side, which becomes narrower towards the peak of the pyramid. The structure contains a PIWI domain with high similarity to argonaute, endoV nuclease and RNase H. The two active sites, each of which contains Mn(2)(+) ion(s) and dAMP, are at the corners of the elliptical channel near the flat face of the dimer. The 3′ OH group of the ribose ring is directed toward the channel entrance, explaining the 5′–3′ nuclease activity of Pf NurA. We provide a DNA binding and cleavage model for Pf NurA. Oxford University Press 2012-03 2011-11-07 /pmc/articles/PMC3300031/ /pubmed/22064858 http://dx.doi.org/10.1093/nar/gkr999 Text en © The Author(s) 2011. 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.
spellingShingle Structural Biology
Chae, Jina
Kim, Young Chang
Cho, Yunje
Crystal structure of the NurA–dAMP–Mn(2+) complex
title Crystal structure of the NurA–dAMP–Mn(2+) complex
title_full Crystal structure of the NurA–dAMP–Mn(2+) complex
title_fullStr Crystal structure of the NurA–dAMP–Mn(2+) complex
title_full_unstemmed Crystal structure of the NurA–dAMP–Mn(2+) complex
title_short Crystal structure of the NurA–dAMP–Mn(2+) complex
title_sort crystal structure of the nura–damp–mn(2+) complex
topic Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3300031/
https://www.ncbi.nlm.nih.gov/pubmed/22064858
http://dx.doi.org/10.1093/nar/gkr999
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