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Literature summary for 3.1.21.10 extracted from

  • Dixit, A.; Ray, K.; Lakowicz, J.R.; Black, L.W.
    Dynamics of the T4 bacteriophage DNA packasome motor: endonuclease VII resolvase release of arrested Y-DNA substrates (2011), J. Biol. Chem., 286, 18878-18889.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.21.10

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Tequatrovirus T4

Organism

Organism UniProt Comment Textmining
Tequatrovirus T4
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information activity with different constructs of Y-DNA under various packaging conditions, T4 endo VII resolvase cleavage sites in Y-DNAs, overview Tequatrovirus T4 ?
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 ?

Synonyms

Synonyms Comment Organism
endonuclease VII resolvase
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 Tequatrovirus T4
T4 endo VII resolvase
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 Tequatrovirus T4
T4 gp49 endonuclease VII resolvase
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 Tequatrovirus T4

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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 assay at Tequatrovirus T4

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Tequatrovirus T4

General Information

General Information Comment Organism
physiological function in vivo the T4 phage packaging motor deals with Y- or X-structures in the replicative concatemer substrate by employing a portal-bound Holliday junction resolvase that trims and releases these DNA roadblocks to packaging. Purified T4 gp49 endonuclease VII resolvase can release DNA compression in vitro in prohead portal packaging motor anchored and arrested Y-DNA substrates. Conformational changes in both the motor proteins and the DNA substrate itself that are associated with the power stroke of the motor are consistent with a proposed linear motor employing a terminal-to-portal DNA grip-and-release mechanism Tequatrovirus T4