Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins

A 3.3 MDa macromolecular cage between two Escherichia coli proteins with seemingly incompatible symmetries–the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI–is reconstructed by cryo-electron microscopy to 11 Å resolution. Combined with a 7.5 Å resolution reconstruc...

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Autores principales: Malet, Hélène, Liu, Kaiyin, El Bakkouri, Majida, Chan, Sze Wah Samuel, Effantin, Gregory, Bacia, Maria, Houry, Walid A, Gutsche, Irina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2014
Materias:
Biophysics and Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4145799/
https://www.ncbi.nlm.nih.gov/pubmed/25097238
http://dx.doi.org/10.7554/eLife.03653
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author Malet, Hélène
Liu, Kaiyin
El Bakkouri, Majida
Chan, Sze Wah Samuel
Effantin, Gregory
Bacia, Maria
Houry, Walid A
Gutsche, Irina
author_facet Malet, Hélène
Liu, Kaiyin
El Bakkouri, Majida
Chan, Sze Wah Samuel
Effantin, Gregory
Bacia, Maria
Houry, Walid A
Gutsche, Irina
author_sort Malet, Hélène
collection PubMed
description A 3.3 MDa macromolecular cage between two Escherichia coli proteins with seemingly incompatible symmetries–the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI–is reconstructed by cryo-electron microscopy to 11 Å resolution. Combined with a 7.5 Å resolution reconstruction of the minimal complex between LdcI and the LdcI-binding domain of RavA, and the previously solved crystal structures of the individual components, this work enables to build a reliable pseudoatomic model of this unusual architecture and to identify conformational rearrangements and specific elements essential for complex formation. The design of the cage created via lateral interactions between five RavA rings is unique for the diverse AAA+ ATPase superfamily. DOI: http://dx.doi.org/10.7554/eLife.03653.001
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spelling pubmed-41457992014-08-28 Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins Malet, Hélène Liu, Kaiyin El Bakkouri, Majida Chan, Sze Wah Samuel Effantin, Gregory Bacia, Maria Houry, Walid A Gutsche, Irina eLife Biophysics and Structural Biology A 3.3 MDa macromolecular cage between two Escherichia coli proteins with seemingly incompatible symmetries–the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI–is reconstructed by cryo-electron microscopy to 11 Å resolution. Combined with a 7.5 Å resolution reconstruction of the minimal complex between LdcI and the LdcI-binding domain of RavA, and the previously solved crystal structures of the individual components, this work enables to build a reliable pseudoatomic model of this unusual architecture and to identify conformational rearrangements and specific elements essential for complex formation. The design of the cage created via lateral interactions between five RavA rings is unique for the diverse AAA+ ATPase superfamily. DOI: http://dx.doi.org/10.7554/eLife.03653.001 eLife Sciences Publications, Ltd 2014-08-05 /pmc/articles/PMC4145799/ /pubmed/25097238 http://dx.doi.org/10.7554/eLife.03653 Text en Copyright © 2014, Malet et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biophysics and Structural Biology
Malet, Hélène
Liu, Kaiyin
El Bakkouri, Majida
Chan, Sze Wah Samuel
Effantin, Gregory
Bacia, Maria
Houry, Walid A
Gutsche, Irina
Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
title Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
title_full Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
title_fullStr Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
title_full_unstemmed Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
title_short Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins
title_sort assembly principles of a unique cage formed by hexameric and decameric e. coli proteins
topic Biophysics and Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4145799/
https://www.ncbi.nlm.nih.gov/pubmed/25097238
http://dx.doi.org/10.7554/eLife.03653
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