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Literature summary for 3.5.1.119 extracted from

  • ึzcelik, D.; Barandun, J.; Schmitz, N.; Sutter, M.; Guth, E.; Damberger, F.F.; Allain, F.H.; Ban, N.; Weber-Ban, E.
    Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway (2012), Nat. Commun., 3, 1014.
    View publication on PubMed
Search for more literature for 3.5.1.119

Cloned(Commentary)

Cloned (Comment) Organism
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 Acidothermus cellulolyticus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the enzyme with ATP, protein (Pup) ligase PafA and the depupylase/deamidase Dop are are close structural homologues Acidothermus cellulolyticus
structure of full-length Dop, to 2.6 A resolution and to 2.85 A resolution in complex with ATP. The active site is located on the concave surface of the beta-sheet with the nucleotide bound in a deep pocket. A conserved groove leading into the active site could play a role in Pup-binding Acidothermus cellulolyticus

Organism

Organism UniProt Comment Textmining
Acidothermus cellulolyticus A0LU48
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Acidothermus cellulolyticus A0LU49
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Acidothermus cellulolyticus ATCC 43068 A0LU48
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Acidothermus cellulolyticus ATCC 43068 A0LU49
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Synonyms

Synonyms Comment Organism
deamidase/depupylase Dop
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 Acidothermus cellulolyticus

General Information

General Information Comment Organism
metabolism pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination Acidothermus cellulolyticus