8SGX

Leishmania tarentolae propionyl-CoA carboxylase (alpha-4-beta-6)

8SGX の概要

• エントリーDOI: 10.2210/pdb8sgx/pdb
• EMDBエントリー: 40472
• 分子名称: Propionyl-coa carboxylase beta chain, putative, propionyl-CoA carboxylase, 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL (3 entities in total)
• 機能のキーワード: multienzyme complex, carboxylase, ligase
• 由来する生物種: Leishmania tarentolae; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 616004.20

構造登録者

Lee, J.K.J.,Liu, Y.T.,Hu, J.J.,Aphasizheva, I.,Aphasizhev, R.,Zhou, Z.H. (登録日: 2023-04-13, 公開日: 2023-05-17, 最終更新日: 2024-06-19)

主引用文献

Lee, J.K.J.,Liu, Y.T.,Hu, J.J.,Aphasizheva, I.,Aphasizhev, R.,Zhou, Z.H.
CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics.
J Struct Biol X, 7:100088-100088, 2023

PubMed Abstract: Propionyl-CoA carboxylase (PCC) is a multienzyme complex consisting of up to six α-subunits and six β-subunits. Belonging to a metabolic pathway converging on the citric acid cycle, it is present in most forms of life and irregularities in its assembly lead to serious illness in humans, known as propionic acidemia. Here, we report the cryogenic electron microscopy (cryoEM) structures and assembly of different oligomeric isomers of endogenous PCC from the parasitic protozoan (LtPCC). These structures and their statistical distribution reveal the mechanics of PCC assembly and disassembly at equilibrium. We show that, in solution, endogenous LtPCC β-subunits form stable homohexamers, to which different numbers of α-subunits attach. Sorting LtPCC particles into seven classes (i.e., oligomeric formulae αβ, αβ, αβ, αβ, αβ, αβ, αβ) enables formulation of a model for PCC assembly. Our results suggest how multimerization regulates PCC enzymatic activity and showcase the utility of cryoEM in revealing the statistical mechanics of reaction pathways.

PubMed: 37128595
DOI: 10.1016/j.yjsbx.2023.100088

実験手法

ELECTRON MICROSCOPY (10.3 Å)