| Title |
Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution / |
| Authors |
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 |
| DOI |
10.1093/nar/gkt713 |
| Full Text |
|
| Is Part of |
Nucleic acids research.. Oxford : Oxford University press. 2013, vol. 41, no. 20, p. 9396-9410.. ISSN 0305-1048 |
| Keywords [eng] |
viruses ; RNA ; genome ; proteins |
| Abstract [eng] |
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 singlestranded RNA genomic precursors into the procapsid. We previously dissected the mechanism of RNA translocation for one such phage, φ12, and have now investigated three further highly divergent, cystoviral P4 NTPases (from φ6, φ8 and φ13). 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 φ8 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 φ12 P4, a C-terminal residue, serine 282, forms a specific hydrogen bond to the N7 of purines ring to confer purine specificity for the φ12 enzyme. |
| Published |
Oxford : Oxford University press |
| Type |
Journal article |
| Language |
English |
| Publication date |
2013 |
| CC license |
|
