1. Structural insight into the role of thiolase from Fusobacterium nucleatum.
- Author
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He S, Bai X, and Xu Y
- Subjects
- Acetyl Coenzyme A, Cysteine metabolism, Fatty Acids, Fusobacterium nucleatum metabolism, Acetyl-CoA C-Acetyltransferase chemistry
- 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., Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Yongbin Xu reports financial support, administrative support, article publishing charges, and equipment, drugs, or supplies were provided by Natural Science Foundation of Liaoning Province., (Copyright © 2023 Elsevier Inc. All rights reserved.)
- Published
- 2023
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