8K1C

Structural insight into the role of acetyl-CoA acetyltransferase from Fusobacterium nucleatum

Summary for 8K1C

• Entry DOI: 10.2210/pdb8k1c/pdb
• Descriptor: Acetyl-CoA acetyltransferase (2 entities in total)
• Functional Keywords: acetyl-coa acetyltransferase, transferase
• Biological source: Fusobacterium nucleatum subsp. nucleatum ATCC 25586
• Total number of polymer chains: 4
• Total formula weight: 169763.81

Authors

He, S.R.,Bai, X.,Zhang, J.,Zhao, Z.D. (deposition date: 2023-07-10, release date: 2023-08-02, Last modification date: 2025-03-19)

Primary citation

He, S.,Bai, X.,Xu, Y.
Structural insight into the role of thiolase from Fusobacterium nucleatum.
Biochem.Biophys.Res.Commun., 688:149151-149151, 2023

PubMed Abstract: Fusobacterium nucleatum (F. nucleatum) is an anaerobic gram-negative bacterium that was previously thought to be related to the progression of colorectal cancer. In F. nucleatum, thiolase participates in fatty acid metabolism, and it can catalyse the transfer of an acetyl group from acetyl-CoA to another molecule, typically a fatty acid or another molecule in the synthesis of lipids. To gain deeper insight into the molecular mechanism governing the function of thiolase in F. nucleatum (Fn0495), we herein report the structure of Fn0495. The monomer of Fn0495 consists of three subdomains, namely, the N-terminal domain (residues 1-117 and 252-270), the C-terminal domain (residues 273-393), and the loop domain (residues 118-251). Fn0495 shows a unique difference in the charge and structure of the substrate binding pocket compared with homologous proteins. This research found three conserved residues (Cys88, His357, and Cys387) in Fn0495 arranged near a potential substrate binding pocket. In this study, the conformational changes between the covering loop, catalytic cysteine loop, regulatory determinant region, and homologous protein were compared. These results will enhance our understanding of the molecular characteristics and roles of the thiolase family.

PubMed: 37951156
DOI: 10.1016/j.bbrc.2023.149151

Experimental method

X-RAY DIFFRACTION (1.894 Å)