Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase.

ABSTRACT: 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. α₆β₆ 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 α₆β₆ LtMCCs onto the exterior α-trimer of the terminal LtMCC. This sta

SUBMITTER: Hu JJ 

PROVIDER: S-EPMC9825669 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature