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TitleDiscovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase.
Journal, issue, pagesStructure, Vol. 31, Issue 1, Page 100-110.e4, Year 2023
Publish dateJan 5, 2023
AuthorsJason J Hu / Jane K J Lee / Yun-Tao Liu / Clinton Yu / Lan Huang / Inna Aphasizheva / Ruslan Aphasizhev / Z Hong Zhou /
PubMed Abstract3-methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent mitochondrial enzyme necessary for leucine catabolism in most organisms. While the crystal structure of recombinant bacterial MCC has been ...3-methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent mitochondrial enzyme necessary for leucine catabolism in most organisms. While the crystal structure of recombinant bacterial MCC has been characterized, the structure and potential polymerization of native MCC remain elusive. Here, we discovered that native MCC from Leishmania tarentolae (LtMCC) forms filaments, and determined the structures of different filament regions at 3.4, 3.9, and 7.3 Å resolution using cryoEM. αβ LtMCCs assemble in a twisted-stacks architecture, manifesting as supramolecular rods up to 400 nm. Filamentous LtMCCs bind biotin non-covalently and lack coenzyme A. Filaments elongate by stacking αβ LtMCCs onto the exterior α-trimer of the terminal LtMCC. This stacking immobilizes the biotin carboxylase domains, sequestering the enzyme in an inactive state. Our results support a new model for LtMCC catalysis, termed the dual-swinging-domains model, and cast new light on the function of polymerization in the carboxylase superfamily and beyond.
External linksStructure / PubMed:36543169 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 7.3 Å
Structure data

28846

8f3d

EMDB-28846, PDB-8f3d:
3-methylcrotonyl-CoA carboxylase in filament, beta-subunit centered
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-28847: 3-methylcrotonyl-CoA carboxylase in filaments, filament termini
Method: EM (single particle) / Resolution: 7.3 Å

28849

8f41

EMDB-28849, PDB-8f41:
3-methylcrotonyl-CoA carboxylase in filament, alpha-subunit centered
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-BTI:
5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL

Source
  • leishmania tarentolae (eukaryote)
KeywordsLIGASE / enzyme / multienzyme / multi-enzyme / biotin-dependent / leucine catabolism / PROTEIN FIBRIL

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