3IL4

Structure of E. faecalis FabH in complex with acetyl CoA

3IL4 の概要

• エントリーDOI: 10.2210/pdb3il4/pdb
• 関連するPDBエントリー: 3IL3 3IL5 3IL6 3IL7 3IL9
• 分子名称: 3-oxoacyl-[acyl-carrier-protein] synthase 3, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: fabh, fatty acid biosynthesis, antibiotic, acyltransferase, cytoplasm, lipid synthesis, multifunctional enzyme, transferase
• 由来する生物種: Enterococcus faecalis
• 細胞内の位置: Cytoplasm : Q820T1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 143716.94

構造登録者

Gajiwala, K.S.,Margosiak, S.,Lu, J.,Cortez, J.,Su, Y.,Nie, Z.,Appelt, K. (登録日: 2009-08-06, 公開日: 2009-08-25, 最終更新日: 2024-11-20)

主引用文献

Gajiwala, K.S.,Margosiak, S.,Lu, J.,Cortez, J.,Su, Y.,Nie, Z.,Appelt, K.
Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
Febs Lett., 583:2939-2946, 2009

PubMed Abstract: FabH (beta-ketoacyl-acyl carrier protein synthase III) is unique in that it initiates fatty acid biosynthesis, is inhibited by long-chain fatty acids providing means for feedback control of the process, and dictates the fatty acid profile of the organism by virtue of its substrate specificity. We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter-species diversity in the substrate specificities of these enzymes.

PubMed: 19665020
DOI: 10.1016/j.febslet.2009.08.001

実験手法

X-RAY DIFFRACTION (3 Å)