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Literature summary for 3.1.21.10 extracted from

  • Middleton, C.L.; Parker, J.L.; Richard, D.J.; White, M.F.; Bond, C.S.
    Substrate recognition and catalysis by the Holliday junction resolving enzyme Hje (2004), Nucleic Acids Res., 32, 5442-5451.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop method at 20°C Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
S30A serine 30 on a flexible loop is catalytically essential, mutants show a decrease in catalytic rate of 3-4 orders of magnitude Saccharolobus solfataricus
S30C serine 30 on a flexible loop is catalytically essential, mutants show a decrease in catalytic rate of 3-4 orders of magnitude Saccharolobus solfataricus
S30T has a slightly higher activity than mutants S30A and S30C but is still severely compromised Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O Holliday structure, junction Jbm5, catalytic site of Hje close to the N-terminus of strand betaB and a bend in betaC Saccharolobus solfataricus ?
-
?

Subunits

Subunits Comment Organism
dimer crystallographic 2fold rotation axis, Se-targeted SAD methods, dimeric in solution and in crystal Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
Hje
-
Saccharolobus solfataricus
Holliday junction endonuclease
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Saccharolobus solfataricus