The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase

DNA glycosylases are lesion-specific enzymes that recognize specific nucleobase damages and catalyze their excision through cleavage of the glycosidic bond. Here, the authors present the crystal structures of human 8-oxoguanine (oxoG) DNA glycosylase bound to undamaged DNA and to DNA containing an i...

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Main Authors: Uddhav K. Shigdel, Victor Ovchinnikov, Seung-Joo Lee, Jenny A. Shih, Martin Karplus, Kwangho Nam, Gregory L. Verdine
Format: Article
Language:English
Published: Nature Portfolio 2020-09-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-18290-2
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author Uddhav K. Shigdel
Victor Ovchinnikov
Seung-Joo Lee
Jenny A. Shih
Martin Karplus
Kwangho Nam
Gregory L. Verdine
author_facet Uddhav K. Shigdel
Victor Ovchinnikov
Seung-Joo Lee
Jenny A. Shih
Martin Karplus
Kwangho Nam
Gregory L. Verdine
author_sort Uddhav K. Shigdel
collection DOAJ
description DNA glycosylases are lesion-specific enzymes that recognize specific nucleobase damages and catalyze their excision through cleavage of the glycosidic bond. Here, the authors present the crystal structures of human 8-oxoguanine (oxoG) DNA glycosylase bound to undamaged DNA and to DNA containing an intrahelical oxoG lesion and further analyse these structures with molecular dynamics simulations, which allows them to characterise the base-extrusion pathways.
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spelling doaj.art-60b39eb87d0b47c4a0f3eab9bd903e6e2022-12-21T22:59:22ZengNature PortfolioNature Communications2041-17232020-09-011111810.1038/s41467-020-18290-2The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylaseUddhav K. Shigdel0Victor Ovchinnikov1Seung-Joo Lee2Jenny A. Shih3Martin Karplus4Kwangho Nam5Gregory L. Verdine6Department of Stem Cell and Regenerative Biology, Harvard UniversityDepartment of Chemistry and Chemical Biology, Harvard UniversityDepartment of Stem Cell and Regenerative Biology, Harvard UniversityDepartment of Stem Cell and Regenerative Biology, Harvard UniversityDepartment of Chemistry and Chemical Biology, Harvard UniversityDepartment of Chemistry and Biochemistry, University of Texas at ArlingtonDepartment of Stem Cell and Regenerative Biology, Harvard UniversityDNA glycosylases are lesion-specific enzymes that recognize specific nucleobase damages and catalyze their excision through cleavage of the glycosidic bond. Here, the authors present the crystal structures of human 8-oxoguanine (oxoG) DNA glycosylase bound to undamaged DNA and to DNA containing an intrahelical oxoG lesion and further analyse these structures with molecular dynamics simulations, which allows them to characterise the base-extrusion pathways.https://doi.org/10.1038/s41467-020-18290-2
spellingShingle Uddhav K. Shigdel
Victor Ovchinnikov
Seung-Joo Lee
Jenny A. Shih
Martin Karplus
Kwangho Nam
Gregory L. Verdine
The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
Nature Communications
title The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_full The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_fullStr The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_full_unstemmed The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_short The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_sort trajectory of intrahelical lesion recognition and extrusion by the human 8 oxoguanine dna glycosylase
url https://doi.org/10.1038/s41467-020-18290-2
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