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...

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Main Authors: El Omari, K, Meier, C, Kainov, D, Sutton, G, Grimes, J, Poranen, M, Bamford, D, Tuma, R, Stuart, D, Mancini, E
Format: Journal article
Jezik:English
Izdano: Oxford University Press 2013
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author El Omari, K
Meier, C
Kainov, D
Sutton, G
Grimes, J
Poranen, M
Bamford, D
Tuma, R
Stuart, D
Mancini, E
author_facet El Omari, K
Meier, C
Kainov, D
Sutton, G
Grimes, J
Poranen, M
Bamford, D
Tuma, R
Stuart, D
Mancini, E
author_sort El Omari, K
collection OXFORD
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, 12, and have now investigated three further highly divergent, cystoviral P4 NTPases (from 6, 8 and 13). 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 8 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 12 P4, a C-terminal residue, serine 282, forms a specific hydrogen bond to the N7 of purines ring to confer purine specificity for the 12 enzyme.
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spelling oxford-uuid:4889de1d-aeb4-453f-8c64-3d0d1d1607302022-03-26T15:26:22ZTracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4889de1d-aeb4-453f-8c64-3d0d1d160730EnglishSymplectic Elements at OxfordOxford University Press2013El Omari, KMeier, CKainov, DSutton, GGrimes, JPoranen, MBamford, DTuma, RStuart, DMancini, EMany 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, 12, and have now investigated three further highly divergent, cystoviral P4 NTPases (from 6, 8 and 13). 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 8 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 12 P4, a C-terminal residue, serine 282, forms a specific hydrogen bond to the N7 of purines ring to confer purine specificity for the 12 enzyme.
spellingShingle El Omari, K
Meier, C
Kainov, D
Sutton, G
Grimes, J
Poranen, M
Bamford, D
Tuma, R
Stuart, D
Mancini, E
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
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