Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics
Nsp15 is a uridine specific endoribonuclease present in all coronaviruses. Here, the authors determine the cryo-EM structures of SARS-CoV-2 Nsp15 in the apo and UTP-bound states, which together with biochemical experiments, mass spectrometry and molecular dynamics simulations provide insights into t...
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Nature Portfolio
2021
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oai:doaj.org-article:3b3bd68422cc4508a02721056de1a0822021-12-02T13:57:32ZCryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics10.1038/s41467-020-20608-z2041-1723https://doaj.org/article/3b3bd68422cc4508a02721056de1a0822021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20608-zhttps://doaj.org/toc/2041-1723Nsp15 is a uridine specific endoribonuclease present in all coronaviruses. Here, the authors determine the cryo-EM structures of SARS-CoV-2 Nsp15 in the apo and UTP-bound states, which together with biochemical experiments, mass spectrometry and molecular dynamics simulations provide insights into the catalytic mechanism of Nsp15 and its conformational dynamics.Monica C. PillonMeredith N. FrazierLucas B. DillardJason G. WilliamsSeda KocamanJuno M. KrahnLalith PereraCassandra K. HayneJacob GordonZachary D. StewartMack SobhanyLeesa J. DeterdingAllen L. HsuVenkata P. DandeyMario J. BorgniaRobin E. StanleyNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021) |
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Science Q Monica C. Pillon Meredith N. Frazier Lucas B. Dillard Jason G. Williams Seda Kocaman Juno M. Krahn Lalith Perera Cassandra K. Hayne Jacob Gordon Zachary D. Stewart Mack Sobhany Leesa J. Deterding Allen L. Hsu Venkata P. Dandey Mario J. Borgnia Robin E. Stanley Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics |
description |
Nsp15 is a uridine specific endoribonuclease present in all coronaviruses. Here, the authors determine the cryo-EM structures of SARS-CoV-2 Nsp15 in the apo and UTP-bound states, which together with biochemical experiments, mass spectrometry and molecular dynamics simulations provide insights into the catalytic mechanism of Nsp15 and its conformational dynamics. |
format |
article |
author |
Monica C. Pillon Meredith N. Frazier Lucas B. Dillard Jason G. Williams Seda Kocaman Juno M. Krahn Lalith Perera Cassandra K. Hayne Jacob Gordon Zachary D. Stewart Mack Sobhany Leesa J. Deterding Allen L. Hsu Venkata P. Dandey Mario J. Borgnia Robin E. Stanley |
author_facet |
Monica C. Pillon Meredith N. Frazier Lucas B. Dillard Jason G. Williams Seda Kocaman Juno M. Krahn Lalith Perera Cassandra K. Hayne Jacob Gordon Zachary D. Stewart Mack Sobhany Leesa J. Deterding Allen L. Hsu Venkata P. Dandey Mario J. Borgnia Robin E. Stanley |
author_sort |
Monica C. Pillon |
title |
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics |
title_short |
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics |
title_full |
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics |
title_fullStr |
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics |
title_full_unstemmed |
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics |
title_sort |
cryo-em structures of the sars-cov-2 endoribonuclease nsp15 reveal insight into nuclease specificity and dynamics |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/3b3bd68422cc4508a02721056de1a082 |
work_keys_str_mv |
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