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Literature summary for 6.5.1.1 extracted from

  • Cuneo, M.J.; Gabel, S.A.; Krahn, J.M.; Ricker, M.A.; London, R.E.
    The structural basis for partitioning of the XRCC1/DNA ligase III-alpha BRCT-mediated dimer complexes (2011), Nucleic Acids Res., 39, 7816-7827.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-DE3-RIL cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
X1BRCTb complexed with L3BRCT Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P49916
-
-

Purification (Commentary)

Purification (Comment) Organism
immobilized metal affinity column chromatography and Superdex S75 gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
Homo sapiens AMP + diphosphate + (deoxyribonucleotide)m+n
-
?
additional information for efficient ligation, ligase III-alpha is constitutively bound to the scaffolding protein XRCC1 through interactions between the C-terminal BRCT domains of each protein Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Homo sapiens

Synonyms

Synonyms Comment Organism
DNA ligase III
-
Homo sapiens
L3BRCT C-terminal ligase III-alpha BRCT domain Homo sapiens
ligase III-alpha
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens