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.

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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	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ubiquitin]-L-lysine	-	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	-	Escherichia coli

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Release 2023.1 (January 2023)