Literature summary for 2.8.2.36 extracted from

Shi, R.; Munger, C.; Kalan, L.; Sulea, T.; Wright, G.D.; Cygler, M.
Sulfonation of glycopeptide antibiotics by sulfotransferase StaL depends on conformational flexibility of aglycone scaffold (2012), Proc. Natl. Acad. Sci. USA, 109, 11824-11829.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Streptomyces toyocaensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the ternary complex of bacterial sulfotransferase StaL with the cofactor product 3'-phosphoadenosine 5'-phosphate and desulfo-A47934 aglycone substrate. Desulfo-A47934 binds with the hydroxyl group on the 4-hydroxyphenylglycine in residue 1 directed toward the 3'-phosphoadenosine 5'-phosphate and hydrogen-bonded to the catalytic His67. Homodimeric StaL can accommodate glycopeptide antiiotic substrate in only one of the two active sites because of potential steric clashes. The aglycone substrate demonstrates a flattened conformation	Streptomyces toyocaensis

Crystallization (Comment)

Organism

crystal structure of the ternary complex of bacterial sulfotransferase StaL with the cofactor product 3'-phosphoadenosine 5'-phosphate and desulfo-A47934 aglycone substrate. Desulfo-A47934 binds with the hydroxyl group on the 4-hydroxyphenylglycine in residue 1 directed toward the 3'-phosphoadenosine 5'-phosphate and hydrogen-bonded to the catalytic His67. Homodimeric StaL can accommodate glycopeptide antiiotic substrate in only one of the two active sites because of potential steric clashes. The aglycone substrate demonstrates a flattened conformation

Streptomyces toyocaensis

Organism

Organism	UniProt	Comment	Textmining
Streptomyces toyocaensis	Q8KLM3	-	-

Synonyms

Synonyms	Comment	Organism
StaL	-	Streptomyces toyocaensis

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Release 2023.1 (January 2023)