8D1U

E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) with an acetylated cysteine and in complex with oxa(dethia)-Coenzyme A

「6X7S」から置き換えられました

8D1U の概要

• エントリーDOI: 10.2210/pdb8d1u/pdb
• 分子名称: 3-oxoacyl-[acyl-carrier-protein] synthase 3, oxa(dethia)-CoA, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: ketoacyl synthase, substrate analog, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34577.17

構造登録者

Benjamin, A.B.,Stunkard, L.M.,Ling, J.,Nice, J.N.,Lohman, J.R. (登録日: 2022-05-27, 公開日: 2022-06-15, 最終更新日: 2024-10-16)

主引用文献

Benjamin, A.B.,Stunkard, L.M.,Ling, J.,Nice, J.N.,Lohman, J.R.
Structures of chloramphenicol acetyltransferase III and Escherichia coli beta-ketoacylsynthase III co-crystallized with partially hydrolysed acetyl-oxa(dethia)CoA.
Acta Crystallogr.,Sect.F, 79:61-69, 2023

PubMed Abstract: Acetyl coenzyme A (acetyl-CoA) is a reactive metabolite that nonproductively hydrolyzes in a number of enzyme active sites in the crystallization time frame. In order to elucidate the enzyme-acetyl-CoA interactions leading to catalysis, acetyl-CoA substrate analogs are needed. One possible analog for use in structural studies is acetyl-oxa(dethia)CoA (AcOCoA), in which the thioester S atom of CoA is replaced by an O atom. Here, structures of chloramphenicol acetyltransferase III (CATIII) and Escherichia coli ketoacylsynthase III (FabH) from crystals grown in the presence of partially hydrolyzed AcOCoA and the respective nucleophile are presented. Based on the structures, the behavior of AcOCoA differs between the enzymes, with FabH reacting with AcOCoA and CATIII being unreactive. The structure of CATIII reveals insight into the catalytic mechanism, with one active site of the trimer having relatively clear electron density for AcOCoA and chloramphenicol and the other active sites having weaker density for AcOCoA. One FabH structure contains a hydrolyzed AcOCoA product oxa(dethia)CoA (OCoA), while the other FabH structure contains an acyl-enzyme intermediate with OCoA. Together, these structures provide preliminary insight into the use of AcOCoA for enzyme structure-function studies with different nucleophiles.

PubMed: 36862094
DOI: 10.1107/S2053230X23001206

実験手法

X-RAY DIFFRACTION (1.302 Å)