5OW0

Crystal structure of an electron transfer flavoprotein from Geobacter metallireducens

5OW0 の概要

• エントリーDOI: 10.2210/pdb5ow0/pdb
• 分子名称: Electron transfer flavoprotein, beta subunit, Electron transfer flavoprotein, alpha subunit, ADENOSINE MONOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: electron transport, anaerobic, toluene metabolism, fad, amp, flavoprotein
• 由来する生物種: Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59630.51

構造登録者

Essen, L.-O.,Vogt, M.S.,Heider, J.,Koelzer, S.,Peschke, P.,Chowdhury, N.P.,Schuehle, K.,Kleinsorge, D. (登録日: 2017-08-30, 公開日: 2018-10-10, 最終更新日: 2024-10-23)

主引用文献

Vogt, M.S.,Schuhle, K.,Kolzer, S.,Peschke, P.,Chowdhury, N.P.,Kleinsorge, D.,Buckel, W.,Essen, L.O.,Heider, J.
Structural and functional characterization of an electron transfer flavoprotein involved in toluene degradation in strictly anaerobic bacteria.
J.Bacteriol., 2019

PubMed Abstract: ()-Benzylsuccinate is the characteristic initial intermediate of anaerobic toluene metabolism, which is formed by a radical-type addition of toluene to fumarate. Its further degradation proceeds by activation to the coenzyme A (CoA)-thioester and β-oxidation involving a specific ()-2-benzylsuccinyl-CoA dehydrogenase (BbsG) affiliated with the family of acyl-CoA dehydrogenases. In this report, we present the biochemical properties of electron transfer flavoproteins (ETFs) from the strictly anaerobic toluene-degrading species and and the facultatively anaerobic bacterium We determined the X-ray structure of the ETF paralogue involved in toluene metabolism of , revealing strong overall similarities to previously characterized ETF variants but significantly different structural properties in the hinge regions mediating conformational changes. We also show that all strictly anaerobic toluene degraders utilize one of multiple genome-encoded related ETF paralogues, which constitute a distinct clade of similar sequences in the ETF family, for β-oxidation of benzylsuccinate. In contrast, facultatively anaerobic toluene degraders contain only one ETF species, which is utilized in all β-oxidation pathways. Our phylogenetic analysis of the known sequences of the ETF family suggests that at least 36 different clades can be differentiated, which are defined either by the taxonomic group of the respective host species (e.g., clade P for ) or by functional specialization (e.g., clade T for anaerobic toluene degradation). This study documents the involvement of ETF in anaerobic toluene metabolism as the physiological electron acceptor for benzylsuccinyl-CoA dehydrogenase. While toluene-degrading denitrifying proteobacteria use a common ETF species, which is also used for other β-oxidation pathways, obligately anaerobic sulfate- or ferric-iron-reducing bacteria use specialized ETF paralogues for toluene degradation. Based on the structure and sequence conservation of these ETFs, they form a new clade that is only remotely related to the previously characterized members of the ETF family. An exhaustive analysis of the available sequences indicated that the protein family consists of several closely related clades of proven or potential electron-bifurcating ETF species and many deeply branching nonbifurcating clades, which either follow the host phylogeny or are affiliated according to functional criteria.

PubMed: 31405915
DOI: 10.1128/JB.00326-19

実験手法

X-RAY DIFFRACTION (1.7 Å)