PDBsum entry 2oca

Hydrolase

PDB id: 2oca

Contents

Protein chain

494 a.a. *

Waters ×106

* Residue conservation analysis

PDB id:

2oca

Name:

Hydrolase

Title:

The crystal structure of t4 uvsw

Structure:

Atp-dependent DNA helicase uvsw. Chain: a. Synonym: dar protein. Engineered: yes. Mutation: yes

Source:

Enterobacteria phage t4. Organism_taxid: 10665. Gene: uvsw, dar. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.70Å R-factor: 0.217 R-free: 0.250

Authors:

I.D.Kerr,S.W.White

Key ref:

I.D.Kerr et al. (2007). Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4. J Biol Chem, 282, 34392-34400. PubMed id: 17878153 DOI: 10.1074/jbc.M705900200

Date:

20-Dec-06 Release date: 16-Oct-07

Protein chain

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: 10.1074/jbc.M705900200

J Biol Chem 282:34392-34400 (2007)

PubMed id: 17878153

Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4.

I.D.Kerr, S.Sivakolundu, Z.Li, J.C.Buchsbaum, L.A.Knox, R.Kriwacki, S.W.White.

ABSTRACT

The uvsWXY system is implicated in the replication and repair of the bacteriophage T4 genome. Whereas the roles of the recombinase (UvsX) and the recombination mediator protein (UvsY) are known, the precise role of UvsW is unclear. Sequence analysis identifies UvsW as a member of the monomeric SF2 helicase superfamily that translocates nucleic acid substrates via the action of two RecA-like motor domains. Functional homologies to Escherichia coli RecG and biochemical analyses have shown that UvsW interacts with branched nucleic acid substrates, suggesting roles in recombination and the rescue of stalled replication forks. A sequencing error at the 3'-end of the uvsW gene has revealed a second, short open reading frame that encodes a protein of unknown function called UvsW.1. We have determined the crystal structure of UvsW to 2.7A and the NMR solution structure of UvsW.1. UvsW has a four-domain architecture with structural homology to the eukaryotic SF2 helicase, Rad54. A model of the UvsW-ssDNA complex identifies structural elements and conserved residues that may interact with nucleic acid substrates. The NMR solution structure of UvsW.1 reveals a dynamic four-helix bundle with homology to the structure-specific nucleic acid binding module of RecQ helicases.

Selected figure(s)

Figure 3.
Structure of full-length UvsW.A, actual crystal structure showing the molecule in the open conformation. B, structure in the modeled closed conformation in which domains 2A and 2B have been rotated according to the structure of NS3-ssDNA. Each domain is labeled. Key conserved residues within the helicase motifs and the two flexible loops are shown, and these are colored blue and pink to reflect interactions with DNA and nucleotide, respectively. Note that in the closed conformation, the helicase motifs congregate at the domain interface and the two flexible loops are at the top of the molecule. The figures were produced using MOLSCRIPT (57) and rendered with RASTER3D (58).

Figure 5.
Primary sequence of UvsW.1. The sequence is shown in the one-letter code, and the secondary structure elements are indicated by the shaded segments.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 34392-34400) copyright 2007.

Figures were selected by an automated process.