A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family
The structure of Igni18, ancient enzyme from the Crenarchaean species Ignicoccus hospitalis, is solved and characterized by Pérez-García, Chow and colleagues. This structure provides insight as to the evolution of metallo-beta-lactamases and their functions.
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Nature Portfolio
2021
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oai:doaj.org-article:882f23538291485d9a533860520c28aa2021-12-02T14:16:33ZA promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family10.1038/s42003-021-01671-82399-3642https://doaj.org/article/882f23538291485d9a533860520c28aa2021-01-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01671-8https://doaj.org/toc/2399-3642The structure of Igni18, ancient enzyme from the Crenarchaean species Ignicoccus hospitalis, is solved and characterized by Pérez-García, Chow and colleagues. This structure provides insight as to the evolution of metallo-beta-lactamases and their functions.Pablo Perez-GarciaStefanie KobusChristoph G. W. GertzenAstrid HoeppnerNicholas HolzscheckChristoph Heinrich StrunkHarald HuberKarl-Erich JaegerHolger GohlkeFilip KovacicSander H. J. SmitsWolfgang R. StreitJennifer ChowNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Biology (General) QH301-705.5 |
| spellingShingle |
Biology (General) QH301-705.5 Pablo Perez-Garcia Stefanie Kobus Christoph G. W. Gertzen Astrid Hoeppner Nicholas Holzscheck Christoph Heinrich Strunk Harald Huber Karl-Erich Jaeger Holger Gohlke Filip Kovacic Sander H. J. Smits Wolfgang R. Streit Jennifer Chow A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family |
| description |
The structure of Igni18, ancient enzyme from the Crenarchaean species Ignicoccus hospitalis, is solved and characterized by Pérez-García, Chow and colleagues. This structure provides insight as to the evolution of metallo-beta-lactamases and their functions. |
| format |
article |
| author |
Pablo Perez-Garcia Stefanie Kobus Christoph G. W. Gertzen Astrid Hoeppner Nicholas Holzscheck Christoph Heinrich Strunk Harald Huber Karl-Erich Jaeger Holger Gohlke Filip Kovacic Sander H. J. Smits Wolfgang R. Streit Jennifer Chow |
| author_facet |
Pablo Perez-Garcia Stefanie Kobus Christoph G. W. Gertzen Astrid Hoeppner Nicholas Holzscheck Christoph Heinrich Strunk Harald Huber Karl-Erich Jaeger Holger Gohlke Filip Kovacic Sander H. J. Smits Wolfgang R. Streit Jennifer Chow |
| author_sort |
Pablo Perez-Garcia |
| title |
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family |
| title_short |
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family |
| title_full |
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family |
| title_fullStr |
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family |
| title_full_unstemmed |
A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family |
| title_sort |
promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family |
| publisher |
Nature Portfolio |
| publishDate |
2021 |
| url |
https://doaj.org/article/882f23538291485d9a533860520c28aa |
| work_keys_str_mv |
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1718391678984781824 |