1ZOW

Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III

1ZOW の概要

• エントリーDOI: 10.2210/pdb1zow/pdb
• 分子名称: 3-oxoacyl-[acyl-carrier-protein] synthase III (2 entities in total)
• 機能のキーワード: fabh, fatty acid biosynthesis, transferase
• 由来する生物種: Staphylococcus aureus subsp. aureus
• 細胞内の位置: Cytoplasm (Probable): Q8NXE2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 135665.59

構造登録者

Qiu, X.,Choudhry, A.E.,Janson, C.A.,Grooms, M.,Daines, R.A.,Lonsdale, J.T.,Khandekar, S.S. (登録日: 2005-05-15, 公開日: 2005-08-09, 最終更新日: 2023-08-23)

主引用文献

Qiu, X.,Choudhry, A.E.,Janson, C.A.,Grooms, M.,Daines, R.A.,Lonsdale, J.T.,Khandekar, S.S.
Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus.
Protein Sci., 14:2087-2094, 2005

PubMed Abstract: beta-Ketoacyl-ACP synthase III (FabH), an essential enzyme for bacterial viability, catalyzes the initiation of fatty acid elongation by condensing malonyl-ACP with acetyl-CoA. We have determined the crystal structure of FabH from Staphylococcus aureus, a Gram-positive human pathogen, to 2 A resolution. Although the overall structure of S. aureus FabH is similar to that of Escherichia coli FabH, the primer binding pocket in S. aureus FabH is significantly larger than that present in E. coli FabH. The structural differences, which agree with kinetic parameters, provide explanation for the observed varying substrate specificity for E. coli and S. aureus FabH. The rank order of activity of S. aureus FabH with various acyl-CoA primers was as follows: isobutyryl- > hexanoyl- > butyryl- > isovaleryl- >> acetyl-CoA. The availability of crystal structure may aid in designing potent, selective inhibitors of S. aureus FabH.

PubMed: 15987898
DOI: 10.1110/ps.051501605

実験手法

X-RAY DIFFRACTION (2 Å)