Literature summary for 2.1.1.222 extracted from

Zhu, Y.; Wu, B.; Zhang, X.; Fan, X.; Niu, L.; Li, X.; Wang, J.; Teng, M.
Structural and biochemical studies reveal UbiG/Coq3 as a class of novel membrane-binding proteins (2015), Biochem. J., 470, 105-114.

Search for more literature for 2.1.1.222

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
H186A	the mutation completely destroys the interaction of the enzyme with liposomes	Escherichia coli
I177A	the mutation sharply reduces the interaction of the enzyme with liposomes	Escherichia coli
K183A	the mutation nearly completely destroys the interaction of the enzyme with liposomes	Escherichia coli
L178A	the mutation nearly completely destroys the interaction of the enzyme with liposomes	Escherichia coli
L178E	the mutation nearly completely destroys the interaction of the enzyme with liposomes	Escherichia coli
R179A	the mutation sharply reduces the interaction of the enzyme with liposomes	Escherichia coli
V181A	the mutation nearly completely destroys the interaction of the enzyme with liposomes	Escherichia coli
V181A/P182A/K183A/G184A/T185A/H186A	the mutations nearly completely destroy the interaction of the enzyme with liposomes	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Escherichia coli	16020	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P17993	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA column chromatography, HiTrap column chromatography, and Superdex 200 gel filtration	Escherichia coli

Subunits

Subunits	Comment	Organism
monomer	x-ray crystallography	Escherichia coli

Synonyms

Synonyms	Comment	Organism
UbiG	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	dependent on	Escherichia coli

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Release 2023.1 (January 2023)