Literature summary for 2.5.1.15 extracted from

Griffith, E.C.; Wallace, M.J.; Wu, Y.; Kumar, G.; Gajewski, S.; Jackson, P.; Phelps, G.A.; Zheng, Z.; Rock, C.O.; Lee, R.E.; White, S.W.
The structural and functional basis for recurring sulfa drug resistance mutations in Staphylococcus aureus dihydropteroate synthase (2018), Front. Microbiol., 9, 1369 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Staphylococcus aureus

Protein Variants

Protein Variants	Comment	Organism
E208K	mutation restores trimethoprim susceptibility closer to wild-type levels while further increasing sulfonamide resistance	Staphylococcus aureus
F17L	mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim	Staphylococcus aureus
S18L	mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim	Staphylococcus aureus
T51M	mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	O05701	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Staphylococcus aureus

Synonyms

Synonyms	Comment	Organism
DHPS	-	Staphylococcus aureus

General Information

General Information	Comment	Organism
drug target	dihydropteroate synthase is the target of the sulfonamide class of drugs	Staphylococcus aureus

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Release 2023.1 (January 2023)