8JFA

Crystal structure of 3-oxoacyl-ACP reductase FabG in complex with NADPH from Helicobacter pylori

8JFA の概要

• エントリーDOI: 10.2210/pdb8jfa/pdb
• 分子名称: 3-oxoacyl-[acyl-carrier-protein] reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: 3-oxoacyl-acp reductase, fabg, nadph, helicobacter pylori, biosynthetic protein
• 由来する生物種: Helicobacter pylori
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 164549.16

構造登録者

Zhou, J.S.,Zhang, L. (登録日: 2023-05-17, 公開日: 2023-11-15, 最終更新日: 2023-11-22)

主引用文献

Zhou, J.,Zhang, L.,Wang, Y.,Song, W.,Huang, Y.,Mu, Y.,Schmitz, W.,Zhang, S.Y.,Lin, H.,Chen, H.Z.,Ye, F.,Zhang, L.
The Molecular Basis of Catalysis by SDR Family Members Ketoacyl-ACP Reductase FabG and Enoyl-ACP Reductase FabI in Type-II Fatty Acid Biosynthesis.
Angew.Chem.Int.Ed.Engl., 62:e202313109-e202313109, 2023

PubMed Abstract: The short-chain dehydrogenase/reductase (SDR) superfamily members acyl-ACP reductases FabG and FabI are indispensable core enzymatic modules and catalytic orientation controllers in type-II fatty acid biosynthesis. Herein, we report their distinct substrate allosteric recognition and enantioselective reduction mechanisms. FabG achieves allosteric regulation of ACP and NADPH through ACP binding across two adjacent FabG monomers, while FabI follows an irreversible compulsory order of substrate binding in that NADH binding must precede that of ACP on a discrete FabI monomer. Moreover, FabG and FabI utilize a backdoor residue Phe187 or a "rheostat" α8 helix for acyl chain length selection, and their corresponding triad residues Ser142 or Tyr145 recognize the keto- or enoyl-acyl substrates, respectively, facilitating initiation of nucleophilic attack by NAD(P)H. The other two triad residues (Tyr and Lys) mediate subsequent proton transfer and (R)-3-hydroxyacyl- or saturated acyl-ACP production.

PubMed: 37779101
DOI: 10.1002/anie.202313109

実験手法

X-RAY DIFFRACTION (2.55 Å)