4BLO
P4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADP
Summary for 4BLO
| Entry DOI | 10.2210/pdb4blo/pdb |
| Related | 4BLP 4BLQ 4BLR 4BLS 4BLT |
| Descriptor | PACKAGING ENZYME P4, CALCIUM ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | hydrolase, atpase, cystoviridae |
| Biological source | PSEUDOMONAS PHAGE PHI6 (BACTERIOPHAGE PHI6) |
| Cellular location | Virion: P11125 |
| Total number of polymer chains | 12 |
| Total formula weight | 397752.23 |
| Authors | El Omari, K.,Meier, C.,Kainov, D.,Sutton, G.,Grimes, J.M.,Poranen, M.M.,Bamford, D.H.,Tuma, R.,Stuart, D.I.,Mancini, E.J. (deposition date: 2013-05-04, release date: 2013-08-21, Last modification date: 2024-05-08) |
| Primary citation | El Omari, K.,Meier, C.,Kainov, D.,Sutton, G.,Grimes, J.M.,Poranen, M.M.,Bamford, D.H.,Tuma, R.,Stuart, D.I.,Mancini, E.J. Tracking in Atomic Detail the Functional Specializations in Viral Reca Helicases that Occur During Evolution. Nucleic Acids Res., 41:9396-, 2013 Cited by PubMed 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, 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. PubMed: 23939620DOI: 10.1093/NAR/GKT713 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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