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...
Main Authors: | , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2020-09-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-18290-2 |
_version_ | 1828973316560388096 |
---|---|
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. |
first_indexed | 2024-12-14T13:44:29Z |
format | Article |
id | doaj.art-60b39eb87d0b47c4a0f3eab9bd903e6e |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-14T13:44:29Z |
publishDate | 2020-09-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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 |
work_keys_str_mv | AT uddhavkshigdel thetrajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT victorovchinnikov thetrajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT seungjoolee thetrajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT jennyashih thetrajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT martinkarplus thetrajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT kwanghonam thetrajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT gregorylverdine thetrajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT uddhavkshigdel trajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT victorovchinnikov trajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT seungjoolee trajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT jennyashih trajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT martinkarplus trajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT kwanghonam trajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase AT gregorylverdine trajectoryofintrahelicallesionrecognitionandextrusionbythehuman8oxoguaninednaglycosylase |