D
IPR015086

Bacteriophage T4, Gp59, helicase assembly protein, C-terminal

InterPro entry
Short namePhage_T4_Gp59_C
Overlapping
homologous
superfamilies
 

Description

The Bacteriophage T4 gene 59 helicase assembly protein (Gp59) is required for recombination-dependent DNA replication and repair, which is the predominant mode of DNA replication in the late stage of T4 infection. Gp59 accelerates the loading of the T4 gene 41 helicase during DNA synthesis by the T4 replication system in vitro. This protein binds to both T4 gene 41 helicase and T4 gene 32 single-stranded DNA binding protein, and to single and double-stranded DNA
[2]
.

The C-terminal domain of the T4 gene 59 helicase assembly protein consists of seven α-helices with short intervening loops and turns; the surface of the domain contains large regions of exposed hydrophobic residues and clusters of acidic and basic residues. The hydrophobic region on the 'bottom' surface of the domain near the C-terminal helix binds the leading strand DNA, whilst the hydrophobic region on the, top, surface of the domain lies between the two arms of the fork DNA, allowing for T4 gene 41 helicase binding and assembly into a hexameric complex around the lagging strand
[1]
.

References

1.Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 A resolution crystal structure reveals a novel alpha-helical two-domain fold. Mueser TC, Jones CE, Nossal NG, Hyde CC. J. Mol. Biol. 296, 597-612, (2000). View articlePMID: 10669611

2.Mutational analysis of the T4 gp59 helicase loader reveals its sites for interaction with helicase, single-stranded binding protein, and DNA. Dolezal D, Jones CE, Lai X, Brister JR, Mueser TC, Nossal NG, Hinton DM. J Biol Chem 287, 18596-607, (2012). PMID: 22427673

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