7PPS

apo FabB from Pseudomonas aeruginosa with single point mutation C161A

7PPS の概要

• エントリーDOI: 10.2210/pdb7pps/pdb
• 分子名称: 3-oxoacyl-[acyl-carrier-protein] synthase 1, 1,2-ETHANEDIOL, IODIDE ION, ... (5 entities in total)
• 機能のキーワード: fatty acid biosynthesis pathway, fabb, transferase
• 由来する生物種: Pseudomonas aeruginosa PA14
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88896.95

構造登録者

Georgiou, C.,Brenk, R.,Yadrykhinsky, V. (登録日: 2021-09-15, 公開日: 2021-10-13, 最終更新日: 2024-01-31)

主引用文献

Yadrykhins'ky, V.,Georgiou, C.,Brenk, R.
Crystal structure of Pseudomonas aeruginosa FabB C161A, a template for structure-based design for new antibiotics.
F1000Res, 10:-, 2021

PubMed Abstract: : FabB (3-oxoacyl-[acyl-carrier-protein] synthase 1) is part of the fatty acid synthesis II pathway found in bacteria and a potential target for antibiotics. The enzyme catalyses the Claisen condensation of malonyl-ACP (acyl carrier protein) with acyl-ACP via an acyl-enzyme intermediate. Here, we report the crystal structure of the intermediate-mimicking FabB ( FabB) C161A variant. : His-tagged FabB C161A was expressed in Rosetta DE3 pLysS cells, cleaved by TEV protease and purified using affinity and size exclusion chromatography. Commercial screens were used to identify suitable crystallization conditions which were subsequently improved to obtain well diffracting crystals. : We developed a robust and efficient system for recombinant expression of FabB C161A. Conditions to obtain well diffracting crystals were established. The crystal structure of FabB C161A was solved by molecular replacement at 1.3 Å resolution. Binding site comparison between FabB and FabF revealed a conserved malonyl binding site but differences in the fatty acid binding channel. : The FabB C161A crystal structure can be used as a template to facilitate the design of FabB inhibitors.

PubMed: 35136566
DOI: 10.12688/f1000research.74018.2

実験手法

X-RAY DIFFRACTION (1.3 Å)