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Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution
Many complex viruses package their genomes into empty protein shells and bacteriophages of the Cystoviridae family provide some of the simplest models for this. The cystoviral hexameric NTPase, P4, uses chemical energy to translocate single-stranded RNA genomic precursors into the procapsid. We prev...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3814363/ https://www.ncbi.nlm.nih.gov/pubmed/23939620 http://dx.doi.org/10.1093/nar/gkt713 |
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author | El Omari, Kamel Meier, Christoph Kainov, Denis Sutton, Geoff Grimes, Jonathan M. Poranen, Minna M. Bamford, Dennis H. Tuma, Roman Stuart, David I. Mancini, Erika J. |
author_facet | El Omari, Kamel Meier, Christoph Kainov, Denis Sutton, Geoff Grimes, Jonathan M. Poranen, Minna M. Bamford, Dennis H. Tuma, Roman Stuart, David I. Mancini, Erika J. |
author_sort | El Omari, Kamel |
collection | PubMed |
description | Many complex viruses package their genomes into empty protein shells and bacteriophages of the Cystoviridae family provide some of the simplest models for this. The cystoviral hexameric NTPase, P4, uses chemical energy to translocate single-stranded RNA genomic precursors into the procapsid. We previously dissected the mechanism of RNA translocation for one such phage, ɸ12, and have now investigated three further highly divergent, cystoviral P4 NTPases (from ɸ6, ɸ8 and ɸ13). High-resolution crystal structures of the set of P4s allow a structure-based phylogenetic analysis, which reveals that these proteins form a distinct subfamily of the RecA-type ATPases. Although the proteins share a common catalytic core, they have different specificities and control mechanisms, which we map onto divergent N- and C-terminal domains. Thus, the RNA loading and tight coupling of NTPase activity with RNA translocation in ɸ8 P4 is due to a remarkable C-terminal structure, which wraps right around the outside of the molecule to insert into the central hole where RNA binds to coupled L1 and L2 loops, whereas in ɸ12 P4, a C-terminal residue, serine 282, forms a specific hydrogen bond to the N7 of purines ring to confer purine specificity for the ɸ12 enzyme. |
format | Online Article Text |
id | pubmed-3814363 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-38143632013-11-04 Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution El Omari, Kamel Meier, Christoph Kainov, Denis Sutton, Geoff Grimes, Jonathan M. Poranen, Minna M. Bamford, Dennis H. Tuma, Roman Stuart, David I. Mancini, Erika J. Nucleic Acids Res Nucleic Acid Enzymes Many complex viruses package their genomes into empty protein shells and bacteriophages of the Cystoviridae family provide some of the simplest models for this. The cystoviral hexameric NTPase, P4, uses chemical energy to translocate single-stranded RNA genomic precursors into the procapsid. We previously dissected the mechanism of RNA translocation for one such phage, ɸ12, and have now investigated three further highly divergent, cystoviral P4 NTPases (from ɸ6, ɸ8 and ɸ13). High-resolution crystal structures of the set of P4s allow a structure-based phylogenetic analysis, which reveals that these proteins form a distinct subfamily of the RecA-type ATPases. Although the proteins share a common catalytic core, they have different specificities and control mechanisms, which we map onto divergent N- and C-terminal domains. Thus, the RNA loading and tight coupling of NTPase activity with RNA translocation in ɸ8 P4 is due to a remarkable C-terminal structure, which wraps right around the outside of the molecule to insert into the central hole where RNA binds to coupled L1 and L2 loops, whereas in ɸ12 P4, a C-terminal residue, serine 282, forms a specific hydrogen bond to the N7 of purines ring to confer purine specificity for the ɸ12 enzyme. Oxford University Press 2013-11 2013-08-10 /pmc/articles/PMC3814363/ /pubmed/23939620 http://dx.doi.org/10.1093/nar/gkt713 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Nucleic Acid Enzymes El Omari, Kamel Meier, Christoph Kainov, Denis Sutton, Geoff Grimes, Jonathan M. Poranen, Minna M. Bamford, Dennis H. Tuma, Roman Stuart, David I. Mancini, Erika J. Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution |
title | Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution |
title_full | Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution |
title_fullStr | Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution |
title_full_unstemmed | Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution |
title_short | Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution |
title_sort | tracking in atomic detail the functional specializations in viral reca helicases that occur during evolution |
topic | Nucleic Acid Enzymes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3814363/ https://www.ncbi.nlm.nih.gov/pubmed/23939620 http://dx.doi.org/10.1093/nar/gkt713 |
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