PDBsum entry 4iee

Viral protein

PDB id: 4iee

Contents

Protein chain

452 a.a.

Ligands

AGS

Metals

_MG

Waters ×386

PDB id:

4iee

Name:

Viral protein

Title:

Crystal structure of the large terminase subunit gp2 of bacterial virus sf6 complexed with atp-r-s

Structure:

Gene 2 protein. Chain: a. Engineered: yes

Source:

Shigella phage sf6. Shigella flexneri bacteriophage vi. Organism_taxid: 10761. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.89Å R-factor: 0.168 R-free: 0.208

Authors:

H.Zhao,T.Christensen,Y.Kamau,L.Tang

Key ref:

H.Zhao et al. (2013). Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage. Proc Natl Acad Sci U S A, 110, 8075-8080. PubMed id: 23630261 DOI: 10.1073/pnas.1301133110

Date:

13-Dec-12 Release date: 01-May-13

Protein chain

Q716H3  (Q716H3_BPSFV) -  Gene 2 protein from Shigella phage Sf6

Seq: 470 a.a.

Struc: 452 a.a.

DOI no: 10.1073/pnas.1301133110

Proc Natl Acad Sci U S A 110:8075-8080 (2013)

PubMed id: 23630261

Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage.

H.Zhao, T.E.Christensen, Y.N.Kamau, L.Tang.

ABSTRACT

Many DNA viruses use powerful molecular motors to cleave concatemeric viral DNA into genome-length units and package them into preformed procapsid powered by ATP hydrolysis. Here we report the structures of the DNA-packaging motor gp2 of bacteriophage Sf6, which reveal a unique clade of RecA-like ATPase domain and an RNase H-like nuclease domain tethered by a regulatory linker domain, exhibiting a strikingly distinct domain arrangement. The gp2 structures complexed with nucleotides reveal, at the atomic detail, the catalytic center embraced by the ATPase domain and the linker domain. The gp2 nuclease activity is modulated by the ATPase domain and is stimulated by ATP. An extended DNA-binding surface is formed by the linker domain and the nuclease domain. These results suggest a unique mechanism for translation of chemical reaction into physical motion of DNA and provide insights into coordination of DNA translocation and cleavage in a viral DNA-packaging motor, which may be achieved via linker-domain-mediated interdomain communication driven by ATP hydrolysis.