Literature summary extracted from
Gomez Garcia, I.; Stevenson, C.E.; Uson, I.; Freel Meyers, C.L.; Walsh, C.T.; Lawson, D.M.
The crystal structure of the novobiocin biosynthetic enzyme NovP: the first representative structure for the TylF O-methyltransferase superfamily (2010), J. Mol. Biol., 395, 390-407.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.1.1.285 |
high resolution crystal structure of NovP as a binary complex with its desmethylated co-substrate, S-adenosyl-L-homocysteine. The structure includes a helical lid region that gates access to the co-substrate binding pocket, and an active centre that contains a 3-Asp putative metal-binding site. A further conserved Asp likely acts as the general base that initiates the reaction by deprotonating the 4-OH group of the noviose unit. Models suggest that NovP is unlikely to tolerate significant modifications at the noviose moiety, but could show increasing substrate promiscuity as a function of the distance of the modification from the methylation site. These observations could inform future attempts to utilise NovP for methylating a range of glycosylated compounds |
Streptomyces niveus |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
2.1.1.285 |
66000 |
- |
gel filtration |
Streptomyces niveus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.1.1.285 |
Streptomyces niveus |
Q9L9F2 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.1.1.285 |
N-terminally His-tagged enzyme |
Streptomyces niveus |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.1.1.285 |
dimer |
- |
Streptomyces niveus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.1.1.285 |
NovP |
- |
Streptomyces niveus |