6KKH

Crystal structure of the oxalate bound malyl-CoA lyase from Roseiflexus castenholzii

6KKH の概要

• エントリーDOI: 10.2210/pdb6kkh/pdb
• 分子名称: HpcH/HpaI aldolase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, OXALATE ION, ... (5 entities in total)
• 機能のキーワード: malyl-coa lyase, cite-like superfamily, roseiflexus castenholzii, conformational changes, lyase
• 由来する生物種: Roseiflexus castenholzii (strain DSM 13941 / HLO8)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 460683.84

構造登録者

Tang, W.R.,Wang, Z.G.,Zhang, C.Y.,Wang, C. (登録日: 2019-07-25, 公開日: 2019-09-04, 最終更新日: 2023-11-22)

主引用文献

Tang, W.,Wang, Z.,Zhang, C.,Wang, C.,Min, Z.,Zhang, X.,Liu, D.,Shen, J.,Xu, X.
The C-terminal domain conformational switch revealed by the crystal structure of malyl-CoA lyase from Roseiflexus castenholzii.
Biochem.Biophys.Res.Commun., 518:72-79, 2019

PubMed Abstract: Malyl-coenzyme A lyase (MCL) is a carbon-carbon bond lyase that catalyzes the reversible cleavage of coenzyme A (CoA) thioesters in multiple carbon metabolic pathways. This enzyme contains a CitE-like TIM barrel and an additional C-terminal domain that undergoes conformational changes upon substrate binding. However, the structural basis underlying these conformational changes is elusive. Here, we report the crystal structure of MCL from the thermophilic photosynthetic bacterium Roseiflexus castenholzii (RfxMCL) in the apo- and oxalate-bound forms at resolutions of 2.50 and 2.65 Å, respectively. Molecular dynamics simulations and structural comparisons with MCLs from other species reveal the deflection of the C-terminal domain to close the adjacent active site pocket in the trimer and contribute active site residues for CoA coordination. The deflection angles of the C-terminal domain are not only related to the occupation but also the type of bound substrates in the adjacent active site pocket. Our work illustrates that a conformational switch of the C-terminal domain accompanies the substrate-binding of MCLs. The results provide a framework for further investigating the reaction mechanism and multifunctionality of MCLs in different carbon metabolic pathways.

PubMed: 31405562
DOI: 10.1016/j.bbrc.2019.08.010

実験手法

X-RAY DIFFRACTION (2.64 Å)