6IHC

Crystal structure of (3R)-Hydroxyacyl-Acyl Carrier Protein Dehydratase(FabZ) Y100A mutant in complex with holo-ACP from Helicobacter pylori

6IHC の概要

• エントリーDOI: 10.2210/pdb6ihc/pdb
• 分子名称: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ, holo-form acyl carrier protein (holo-ACP), CITRIC ACID, ... (5 entities in total)
• 機能のキーワード: dehydrotase, fatty acid biosynthesis, biosynthetic protein
• 由来する生物種: Helicobacter pylori (Campylobacter pylori); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 112243.05

構造登録者

Shen, S.Q.,Zhang, L.,Zhang, L. (登録日: 2018-09-29, 公開日: 2019-04-10, 最終更新日: 2024-11-06)

主引用文献

Shen, S.Q.,Hang, X.D.,Zhuang, J.J.,Zhang, L.,Bi, H.K.,Zhang, L.
A back-door Phenylalanine coordinates the stepwise hexameric loading of acyl carrier protein by the fatty acid biosynthesis enzyme beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ).
Int. J. Biol. Macromol., 128:5-11, 2019

PubMed Abstract: The fatty acid biosynthesis pathway (FAS) was a fundamental procedure to generate a diversity of lipid components for cellular metabolism in bacteria, while the mechanism of substrate recognition remains unclear. The β-hydroxyacyl-acyl carrier protein dehydratase hexamer (FabZ) is an essential module in the elongation cycle of type-II FAS, catalyzing the dehydration of β-hydroxyacyl-lipid substrate carried by the holo form acyl carrier protein (holo-ACP). We previously elucidated an alternating seesaw-like ACP loading manner within a FabZ dimer subunits, mediated by a front-door residue Tyrosine (Tyr100). Here, we demonstrated that a back-door residue Phenylalanine (Phe83) of FabZ regulates the stepwise hexameric loading of ACP. Our finding represents clues as to the dynamic ACP recognition and catalysis mechanism of dehydratase in fatty acid biosynthesis, and provides critical information for developing antimicrobials targeting the dehydratase module in fatty acid biosynthesis pathway.

PubMed: 30677439
DOI: 10.1016/j.ijbiomac.2019.01.094

実験手法

X-RAY DIFFRACTION (2.4 Å)