Literature summary for 1.3.1.39 extracted from

Priyadarshi, A.; Kim, E.; Hwang, K.
Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI), in complex with NADP end triclosan (2010), Proteins Struct. Funct. Bioinform., 78, 480-486.

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo-enzyme and complex with NADPH and inhibitor triclosan. Enzyme is a tetramer. In the apo-form of the SaFabI structure, residues Ile193 to Leu196 form part of a flexible loop adjacent to the active site. In the open conformation, the loop is on the surface of the protein, and does not form any secondary structure or contribute to inhibitor or cofactor binding. The substrate-binding loop of the holo-enzyme containing Ser197, Val201 and Phe204 has a closed conformation	Staphylococcus aureus

Crystallization (Comment)

Organism

apo-enzyme and complex with NADPH and inhibitor triclosan. Enzyme is a tetramer. In the apo-form of the SaFabI structure, residues Ile193 to Leu196 form part of a flexible loop adjacent to the active site. In the open conformation, the loop is on the surface of the protein, and does not form any secondary structure or contribute to inhibitor or cofactor binding. The substrate-binding loop of the holo-enzyme containing Ser197, Val201 and Phe204 has a closed conformation

Staphylococcus aureus

Inhibitors

Inhibitors	Comment	Organism	Structure
triclosan	affinity varies with pH-value	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	Q6GI75	-	-

Synonyms

Synonyms	Comment	Organism
FabI	-	Staphylococcus aureus

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Staphylococcus aureus

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Release 2023.1 (January 2023)