5JFM

Crystal structure of Rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-CoA

5JFM の概要

• エントリーDOI: 10.2210/pdb5jfm/pdb
• 関連するPDBエントリー: 5JFL 5JFN
• 分子名称: Aldehyde dehydrogenase, propionyl Coenzyme A, COENZYME A, ... (4 entities in total)
• 機能のキーワード: acylating aldehyde dehydrogenase, propionylcysteine, bacterial microcompartments, oxidoreductase
• 由来する生物種: Rhodopseudomonas palustris (strain BisB18)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 450720.96

構造登録者

Zarzycki, J.,Sutter, M.,Kerfeld, C.A. (登録日: 2016-04-19, 公開日: 2017-03-01, 最終更新日: 2023-09-27)

主引用文献

Zarzycki, J.,Sutter, M.,Cortina, N.S.,Erb, T.J.,Kerfeld, C.A.
In Vitro Characterization and Concerted Function of Three Core Enzymes of a Glycyl Radical Enzyme - Associated Bacterial Microcompartment.
Sci Rep, 7:42757-42757, 2017

PubMed Abstract: Many bacteria encode proteinaceous bacterial microcompartments (BMCs) that encapsulate sequential enzymatic reactions of diverse metabolic pathways. Well-characterized BMCs include carboxysomes for CO-fixation, and propanediol- and ethanolamine-utilizing microcompartments that contain B-dependent enzymes. Genes required to form BMCs are typically organized in gene clusters, which promoted their distribution across phyla by horizontal gene transfer. Recently, BMCs associated with glycyl radical enzymes (GREs) were discovered; these are widespread and comprise at least three functionally distinct types. Previously, we predicted one type of these GRE-associated microcompartments (GRMs) represents a B-independent propanediol-utilizing BMC. Here we functionally and structurally characterize enzymes of the GRM of Rhodopseudomonas palustris BisB18 and demonstrate their concerted function in vitro. The GRM signature enzyme, the GRE, is a dedicated 1,2-propanediol dehydratase with a new type of intramolecular encapsulation peptide. It forms a complex with its activating enzyme and, in conjunction with an aldehyde dehydrogenase, converts 1,2-propanediol to propionyl-CoA. Notably, homologous GRMs are also encoded in pathogenic Escherichia coli strains. Our high-resolution crystal structures of the aldehyde dehydrogenase lead to a revised reaction mechanism. The successful in vitro reconstitution of a part of the GRM metabolism provides insights into the metabolic function and steps in the assembly of this BMC.

PubMed: 28202954
DOI: 10.1038/srep42757

実験手法

X-RAY DIFFRACTION (2.516 Å)