Cargando…
The solution structure of an anti-CRISPR protein
Bacterial CRISPR–Cas adaptive immune systems use small guide RNAs to protect against phage infection and invasion by foreign genetic elements. We previously demonstrated that a group of Pseudomonas aeruginosa phages encode anti-CRISPR proteins that inactivate the type I-F and I-E CRISPR–Cas systems...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5062604/ https://www.ncbi.nlm.nih.gov/pubmed/27725669 http://dx.doi.org/10.1038/ncomms13134 |
_version_ | 1782459811431972864 |
---|---|
author | Maxwell, Karen L. Garcia, Bianca Bondy-Denomy, Joseph Bona, Diane Hidalgo-Reyes, Yurima Davidson, Alan R. |
author_facet | Maxwell, Karen L. Garcia, Bianca Bondy-Denomy, Joseph Bona, Diane Hidalgo-Reyes, Yurima Davidson, Alan R. |
author_sort | Maxwell, Karen L. |
collection | PubMed |
description | Bacterial CRISPR–Cas adaptive immune systems use small guide RNAs to protect against phage infection and invasion by foreign genetic elements. We previously demonstrated that a group of Pseudomonas aeruginosa phages encode anti-CRISPR proteins that inactivate the type I-F and I-E CRISPR–Cas systems using distinct mechanisms. Here, we present the three-dimensional structure of an anti-CRISPR protein and map a functional surface that is critical for its potent inhibitory activity. The interaction of the anti-CRISPR protein with the CRISPR–Cas complex through this functional surface is proposed to prevent the binding of target DNA. |
format | Online Article Text |
id | pubmed-5062604 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-50626042016-10-27 The solution structure of an anti-CRISPR protein Maxwell, Karen L. Garcia, Bianca Bondy-Denomy, Joseph Bona, Diane Hidalgo-Reyes, Yurima Davidson, Alan R. Nat Commun Article Bacterial CRISPR–Cas adaptive immune systems use small guide RNAs to protect against phage infection and invasion by foreign genetic elements. We previously demonstrated that a group of Pseudomonas aeruginosa phages encode anti-CRISPR proteins that inactivate the type I-F and I-E CRISPR–Cas systems using distinct mechanisms. Here, we present the three-dimensional structure of an anti-CRISPR protein and map a functional surface that is critical for its potent inhibitory activity. The interaction of the anti-CRISPR protein with the CRISPR–Cas complex through this functional surface is proposed to prevent the binding of target DNA. Nature Publishing Group 2016-10-11 /pmc/articles/PMC5062604/ /pubmed/27725669 http://dx.doi.org/10.1038/ncomms13134 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Maxwell, Karen L. Garcia, Bianca Bondy-Denomy, Joseph Bona, Diane Hidalgo-Reyes, Yurima Davidson, Alan R. The solution structure of an anti-CRISPR protein |
title | The solution structure of an anti-CRISPR protein |
title_full | The solution structure of an anti-CRISPR protein |
title_fullStr | The solution structure of an anti-CRISPR protein |
title_full_unstemmed | The solution structure of an anti-CRISPR protein |
title_short | The solution structure of an anti-CRISPR protein |
title_sort | solution structure of an anti-crispr protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5062604/ https://www.ncbi.nlm.nih.gov/pubmed/27725669 http://dx.doi.org/10.1038/ncomms13134 |
work_keys_str_mv | AT maxwellkarenl thesolutionstructureofananticrisprprotein AT garciabianca thesolutionstructureofananticrisprprotein AT bondydenomyjoseph thesolutionstructureofananticrisprprotein AT bonadiane thesolutionstructureofananticrisprprotein AT hidalgoreyesyurima thesolutionstructureofananticrisprprotein AT davidsonalanr thesolutionstructureofananticrisprprotein AT maxwellkarenl solutionstructureofananticrisprprotein AT garciabianca solutionstructureofananticrisprprotein AT bondydenomyjoseph solutionstructureofananticrisprprotein AT bonadiane solutionstructureofananticrisprprotein AT hidalgoreyesyurima solutionstructureofananticrisprprotein AT davidsonalanr solutionstructureofananticrisprprotein |