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8SGY

Leishmania tarentolae propionyl-CoA carboxylase (alpha-5-beta-6)

Summary for 8SGY
Entry DOI10.2210/pdb8sgy/pdb
Related8SGX
EMDB information40472 40473
Descriptorpropionyl-CoA carboxylase, Propionyl-coa carboxylase beta chain, putative, 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL (3 entities in total)
Functional Keywordsmultienzyme complex, carboxylase, ligase
Biological sourceLeishmania tarentolae
More
Total number of polymer chains11
Total formula weight689281.86
Authors
Lee, J.K.J.,Liu, Y.T.,Hu, J.J.,Aphasizheva, I.,Aphasizhev, R.,Zhou, Z.H. (deposition date: 2023-04-13, release date: 2023-05-17, Last modification date: 2024-06-19)
Primary citationLee, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8.62 Å)
Structure validation

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