PDBsum entry 1rif

DNA binding protein

PDB id: 1rif

Contents

Protein chains

282 a.a. *

Metals

_AU ×4

_MG ×3

Waters ×254

* Residue conservation analysis

PDB id:

1rif

Name:

DNA binding protein

Title:

Crystal structure of the uvsw helicase from bacteriophage t4

Structure:

DNA helicase uvsw. Chain: a, b. Synonym: dar protein. Engineered: yes. Mutation: yes

Source:

Enterobacteria phage t4. Organism_taxid: 10665. Gene: uvsw, dar. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.218 R-free: 0.246

Authors:

E.A.Sickmier,S.W.White,K.N.Kreuzer

Key ref:

E.A.Sickmier et al. (2004). The crystal structure of the UvsW helicase from bacteriophage T4. Structure, 12, 583-592. PubMed id: 15062081 DOI: 10.1016/j.str.2004.02.016

Date:

17-Nov-03 Release date: 25-Nov-03

Protein chains

P20703  (UVSW_BPT4) -

Enzyme reactions

• Enzyme class: E.C.3.6.4.12 - Dna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2004.02.016

Structure 12:583-592 (2004)

PubMed id: 15062081

The crystal structure of the UvsW helicase from bacteriophage T4.

E.A.Sickmier, K.N.Kreuzer, S.W.White.

ABSTRACT

In bacteriophage T4, the WXY system repairs DNA damage by a process that involves homologous recombination. This system comprises three proteins, the RecA-like recombination protein UvsX, a recombination mediator protein UvsY, and a helicase UvsW. Here we report the 2.0 A resolution crystal structure of the N-terminal two domains of the UvsW helicase (UvsWNF; residues 1-282). The structure reveals a typical helicase RecA-like domain linked to a small N-terminal alpha/beta domain that likely binds the nucleic acid substrate. The missing C-terminal portion of UvsW almost certainly corresponds to the second RecA-like domain typically found in monomeric helicases. The putative substrate binding domain is unique within the known helicase structures, and it resembles the novel "double-wing" DNA binding domain from the phage T4 MotA transcription factor that mediates the expression of T4 middle genes. The functional implications of this homology for the role of UvsW in T4 DNA metabolism are discussed.

Selected figure(s)

Figure 4.
Figure 4. The UvsW Arginine/Aromatic-Rich Loop(A) A stereoview showing the conformation of the loop and the distinctive residues within the loop.(B) A comparison of the orientations of the loop in molecules A (red) and B (blue) of the crystal asymmetric unit. The two spheres mark the locations of the conserved glycine residues that flank the loop. In this view, the bound dsDNA substrate would be directly below the loop. The figures were produced using MOLSCRIPT (Kraulis, 1991) and rendered with RASTER3D (Merritt and Bacon, 1997).

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 583-592) copyright 2004.

Figure was selected by an automated process.