5CUO

Structure of Rhodopseudomonas palustris PduL - CoA bound form

5CUO の概要

• エントリーDOI: 10.2210/pdb5cuo/pdb
• 関連するPDBエントリー: 5CUP 5CVT
• 分子名称: Phosphate propanoyltransferase, COENZYME A, ZINC ION, ... (4 entities in total)
• 機能のキーワード: enzyme, transferase
• 由来する生物種: Rhodopseudomonas palustris (strain BisB18)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45612.70

構造登録者

Sutter, M.,Erbilgin, O.,Kerfeld, C.A. (登録日: 2015-07-24, 公開日: 2016-03-23, 最終更新日: 2024-03-06)

主引用文献

Erbilgin, O.,Sutter, M.,Kerfeld, C.A.
The Structural Basis of Coenzyme A Recycling in a Bacterial Organelle.
Plos Biol., 14:e1002399-e1002399, 2016

PubMed Abstract: Bacterial Microcompartments (BMCs) are proteinaceous organelles that encapsulate critical segments of autotrophic and heterotrophic metabolic pathways; they are functionally diverse and are found across 23 different phyla. The majority of catabolic BMCs (metabolosomes) compartmentalize a common core of enzymes to metabolize compounds via a toxic and/or volatile aldehyde intermediate. The core enzyme phosphotransacylase (PTAC) recycles Coenzyme A and generates an acyl phosphate that can serve as an energy source. The PTAC predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). Here, we report two high-resolution PduL crystal structures with bound substrates. The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC. Accordingly, PduL and Pta exemplify functional, but not structural, convergent evolution. The PduL structure, in the context of the catalytic core, completes our understanding of the structural basis of cofactor recycling in the metabolosome lumen.

PubMed: 26959993
DOI: 10.1371/journal.pbio.1002399

実験手法

X-RAY DIFFRACTION (1.544 Å)