8F3D

3-methylcrotonyl-CoA carboxylase in filament, beta-subunit centered

8F3D の概要

• エントリーDOI: 10.2210/pdb8f3d/pdb
• EMDBエントリー: 28846
• 分子名称: 3-methylcrotonyl-CoA carboxylase beta-subunit, 3-methylcrotonyl-CoA carboxylase alpha-subunit, 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: enzyme, multienzyme, multi-enzyme, biotin-dependent, leucine catabolism, protein fibril, ligase
• 由来する生物種: Leishmania tarentolae; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 917879.10

構造登録者

Hu, J.J.,Lee, J.K.J.,Liu, Y.T.,Yu, C.,Huang, L.,Afasizheva, I.,Afasizhev, R.,Zhou, Z.H. (登録日: 2022-11-09, 公開日: 2023-01-11, 最終更新日: 2024-06-19)

主引用文献

Hu, J.J.,Lee, J.K.J.,Liu, Y.T.,Yu, C.,Huang, L.,Aphasizheva, I.,Aphasizhev, R.,Zhou, Z.H.
Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase.
Structure, 31:100-110.e4, 2023

PubMed 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. 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.

PubMed: 36543169
DOI: 10.1016/j.str.2022.11.015

実験手法

ELECTRON MICROSCOPY (3.4 Å)