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Provedor de dados: |
ArchiMer
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País: |
France
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Título: |
Structure of an octameric form of the minichromosome maintenance protein from the archaeon Pyrococcus abyssi
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Autores: |
Cannone, Giuseppe
Visentin, Silvia
Palud, Adeline
Henneke, Ghislaine
Spagnolo, Laura
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Data: |
2017-02
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Ano: |
2017
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Resumo: |
Cell division is a complex process that requires precise duplication of genetic material. Duplication is concerted by replisomes. The Minichromosome Maintenance (MCM) replicative helicase is a crucial component of replisomes. Eukaryotic and archaeal MCM proteins are highly conserved. In fact, archaeal MCMs are powerful tools for elucidating essential features of MCM function. However, while eukaryotic MCM2-7 is a heterocomplex made of different polypeptide chains, the MCM complexes of many Archaea form homohexamers from a single gene product. Moreover, some archaeal MCMs are polymorphic, and both hexameric and heptameric architectures have been reported for the same polypeptide. Here, we present the structure of the archaeal MCM helicase from Pyrococcus abyssi in its single octameric ring assembly. To our knowledge, this is the first report of a full-length octameric MCM helicase.
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Tipo: |
Text
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Idioma: |
Inglês
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Identificador: |
http://archimer.ifremer.fr/doc/00373/48434/48701.pdf
http://archimer.ifremer.fr/doc/00373/48434/48702.pdf
DOI:10.1038/srep42019
http://archimer.ifremer.fr/doc/00373/48434/
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Editor: |
Nature Publishing Group
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Formato: |
application/pdf
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Fonte: |
Scientific Reports (2045-2322) (Nature Publishing Group), 2017-02 , Vol. 7 , N. 42019 , P. 1-10
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Direitos: |
The Author(s) 2017. 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 ...
info:eu-repo/semantics/openAccess
restricted use
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