4BLS

P4 PROTEIN FROM BACTERIOPHAGE PHI12 Q278A MUTANT IN COMPLEX WITH AMPcPP

Summary for 4BLS

• Entry DOI: 10.2210/pdb4bls/pdb
• Related: 4BLO 4BLP 4BLQ 4BLR 4BLT 4BWY
• Descriptor: NTPASE P4, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER (2 entities in total)
• Functional Keywords: hydrolase, packaging, cystoviridae
• Biological source: PSEUDOMONAS PHAGE PHI12 (BACTERIOPHAGE PHI12)
• Total number of polymer chains: 3
• Total formula weight: 106795.76

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: 2023-12-20)

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

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: 23939620
DOI: 10.1093/NAR/GKT713

Experimental method

X-RAY DIFFRACTION (2.6 Å)