PDBsum entry 4blr

Hydrolase

PDB id: 4blr

Contents

Protein chains

297 a.a.

Ligands

UTP ×3

DTT

Waters ×640

PDB id:

4blr

Name:

Hydrolase

Title:

P4 protein from bacteriophage phi12 in complex with utp

Structure:

Ntpase p4. Chain: a, b, c. Synonym: phi12 p4. Engineered: yes

Source:

Pseudomonas phage phi12. Bacteriophage phi12. Organism_taxid: 161736. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.90Å R-factor: 0.194 R-free: 0.204

Authors:

K.El Omari,C.Meier,D.Kainov,G.Sutton,J.M.Grimes,M.M.Poranen, D.H.Bamford,R.Tuma,D.I.Stuart,E.J.Mancini

Key ref:

K.El Omari et al. (2013). Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution. Nucleic Acids Res, 41, 9396-9410. PubMed id: 23939620 DOI: 10.1093/nar/gkt713

Date:

04-May-13 Release date: 21-Aug-13

Protein chains

Q94M05  (Q94M05_9VIRU) -  NTPase P4 from Pseudomonas phage phi12

Seq: 331 a.a.

Struc: 297 a.a.

DOI no: 10.1093/nar/gkt713

Nucleic Acids Res 41:9396-9410 (2013)

PubMed id: 23939620

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

K.El Omari, C.Meier, D.Kainov, G.Sutton, J.M.Grimes, M.M.Poranen, D.H.Bamford, R.Tuma, D.I.Stuart, E.J.Mancini.

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.