6SL9

High resolution apo structure of isomerase PaaG

これはPDB形式変換不可エントリーです。

6SL9 の概要

• エントリーDOI: 10.2210/pdb6sl9/pdb
• 分子名称: Enoyl-CoA hydratase/carnithine racemase, GLYCEROL (3 entities in total)
• 機能のキーワード: phenylacetic acid catabolism, isomerase, tropodithietic acid, crotonase
• 由来する生物種: Thermus thermophilus JL-18
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28132.44

構造登録者

Saleem-Batcha, R.,Spieker, M.,Teufel, R. (登録日: 2019-08-19, 公開日: 2019-12-11, 最終更新日: 2024-01-24)

主引用文献

Spieker, M.,Saleem-Batcha, R.,Teufel, R.
Structural and Mechanistic Basis of an Oxepin-CoA Forming Isomerase in Bacterial Primary and Secondary Metabolism.
Acs Chem.Biol., 14:2876-2886, 2019

PubMed Abstract: Numerous aromatic compounds are aerobically degraded in bacteria via the central intermediate phenylacetic acid (paa). In one of the key steps of this widespread catabolic pathway, 1,2-epoxyphenylacetyl-CoA is converted by PaaG into the heterocyclic oxepin-CoA. PaaG thereby elegantly generates an α,β-unsaturated CoA ester that is predisposed to undergo β-oxidation subsequent to hydrolytic ring-cleavage. Moreover, oxepin-CoA serves as a precursor for secondary metabolites (e.g., tropodithietic acid) that act as antibiotics and quorum-sensing signals. Here we verify that PaaG adopts a second role in aromatic catabolism by converting -3,4-didehydroadipoyl-CoA into -2,3-didehydroadipoyl-CoA and corroborate a Δ,Δ-enoyl-CoA isomerase-like proton shuttling mechanism for both distinct substrates. Biochemical and structural investigations of PaaG reveal active site adaptations to the structurally different substrates and provide detailed insight into catalysis and control of stereospecificity. This work elucidates the mechanism of action of unusual isomerase PaaG and sheds new light on the ubiquitous enoyl-CoA isomerases of the crotonase superfamily.

PubMed: 31689071
DOI: 10.1021/acschembio.9b00742

実験手法

X-RAY DIFFRACTION (1.27 Å)