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Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution

DOI: 10.1093/nar/gkt713 DOI Help
PMID: 23939620 PMID Help

Authors: Kamel El Omari (The Wellcome Trust Centre for Human Genetics, University of Oxford) , Christoph Meier (The Wellcome Trust Centre for Human Genetics, University of Oxford) , Denis Kainov (Institute for Molecular Medicine Finland (FIMM), University of Helsinki; Siauliai University) , Geoff C. Sutton (The Wellcome Trust Centre for Human Genetics, University of Oxford) , Jonathan M. Grimes (The Wellcome Trust Centre for Human Genetics, University of Oxford; Diamond Light Source) , Minna M. Poranen (University of Helsinki) , Dennis H. Bamford (University of Helsinki) , Roman Tuma (University of Leeds) , Dave Stuart (Diamond Light Source) , Erika Mancini (The Wellcome Trust Centre for Human Genetics, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nucleic Acids Research

State: Published (Approved)
Published: August 2013

Open Access Open Access

Abstract: 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.

Journal Keywords: Amino; Binding; Cystoviridae; Endodeoxyribonucleases; Evolution; Molecular; Models; Molecular; Nucleotides; Protein; Tertiary; RNA; RNA; Rec; Viral Proteins

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I02-Macromolecular Crystallography

Other Facilities: SRS 14.2 ESRF ID29 ESRF ID14]EH4 ESRF ID14]EH2

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