PDBsum entry 4zni

Viral protein

PDB id: 4zni

Contents

Protein chain

251 a.a.

Ligands

SO4 ×7

Waters ×101

PDB id:

4zni

Name:

Viral protein

Title:

Thermus phage p74-26 large terminase atpase domain (i 2 3 space group)

Structure:

Phage terminase large subunit. Chain: a. Fragment: residues 1-256. Engineered: yes

Source:

Thermus phage p7426. Organism_taxid: 466052. Gene: p74p84. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.10Å R-factor: 0.176 R-free: 0.213

Authors:

B.J.Hilbert,J.A.Hayes,N.P.Stone,C.M.Duffy,B.Sankaran,B.A.Kelch

Key ref:

B.J.Hilbert et al. (2015). Structure and mechanism of the ATPase that powers viral genome packaging. Proc Natl Acad Sci U S A, 112, E3792. PubMed id: 26150523 DOI: 10.1073/pnas.1506951112

Date:

04-May-15 Release date: 08-Jul-15

Protein chain

A7XXR1  (A7XXR1_BP742) -  Terminase, large subunit from Thermus virus P74-26

Seq: 485 a.a.

Struc: 251 a.a.

Enzyme reactions

• Enzyme class 1: E.C.3.1.21.- - ?????
• Enzyme class 2: E.C.3.6.4.- - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.1073/pnas.1506951112

Proc Natl Acad Sci U S A 112:E3792 (2015)

PubMed id: 26150523

Structure and mechanism of the ATPase that powers viral genome packaging.

B.J.Hilbert, J.A.Hayes, N.P.Stone, C.M.Duffy, B.Sankaran, B.A.Kelch.

ABSTRACT

Many viruses package their genomes into procapsids using an ATPase machine that is among the most powerful known biological motors. However, how this motor couples ATP hydrolysis to DNA translocation is still unknown. Here, we introduce a model system with unique properties for studying motor structure and mechanism. We describe crystal structures of the packaging motor ATPase domain that exhibit nucleotide-dependent conformational changes involving a large rotation of an entire subdomain. We also identify the arginine finger residue that catalyzes ATP hydrolysis in a neighboring motor subunit, illustrating that previous models for motor structure need revision. Our findings allow us to derive a structural model for the motor ring, which we validate using small-angle X-ray scattering and comparisons with previously published data. We illustrate the model's predictive power by identifying the motor's DNA-binding and assembly motifs. Finally, we integrate our results to propose a mechanistic model for DNA translocation by this molecular machine.