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Literature summary for 2.3.2.26 extracted from

  • Lin, D.Y.; Diao, J.; Zhou, D.; Chen, J.
    Biochemical and structural studies of a HECT-like ubiquitin ligase from Escherichia coli O157:H7 (2011), J. Biol. Chem., 286, 441-449.
    View publication on PubMed
Search for more literature for 2.3.2.26

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of isoform NleL contains two domains, a beta-helix domain formed by pentapeptide repeats and a bilobed catalytic domain reminiscent of the N- and C-lobe architecture of HECT E3s. The C-lobe adopts a large range of different positions relative to the N-lobe, indicating that the helix linking the two lobes is extremely flexible Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli A0A0H3JDV8
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ubiquitin]-L-lysine
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 Escherichia coli [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ubiquitin]-L-lysine isoform NleL functionally and structurally mimics eukaryotic HECT E3 ligases and catalyzes formation of unanchored polyubiquitin chains using Lys6 and Lys48 linkage. The catalytic cysteine residue forms a thioester intermediate with ubiquitin ?

Synonyms

Synonyms Comment Organism
NleL
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 Escherichia coli