4WYS

Crystal structure of thiolase from Escherichia coli

4WYS の概要

• エントリーDOI: 10.2210/pdb4wys/pdb
• 分子名称: Acetyl-CoA acetyltransferase (2 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P76461
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 166883.19

構造登録者

Kim, S.,Ha, S.C.,Ahn, J.W.,Kim, E.J.,Lim, J.H.,Kim, K.J. (登録日: 2014-11-18, 公開日: 2015-10-07, 最終更新日: 2023-11-08)

主引用文献

Kim, S.,Jang, Y.S.,Ha, S.C.,Ahn, J.W.,Kim, E.J.,Hong Lim, J.,Cho, C.,Shin Ryu, Y.,Kuk Lee, S.,Lee, S.Y.,Kim, K.J.
Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum
Nat Commun, 6:8410-8410, 2015

PubMed Abstract: Thiolase is the first enzyme catalysing the condensation of two acetyl-coenzyme A (CoA) molecules to form acetoacetyl-CoA in a dedicated pathway towards the biosynthesis of n-butanol, an important solvent and biofuel. Here we elucidate the crystal structure of Clostridium acetobutylicum thiolase (CaTHL) in its reduced/oxidized states. CaTHL, unlike those from other aerobic bacteria such as Escherichia coli and Zoogloea ramegera, is regulated by the redox-switch modulation through reversible disulfide bond formation between two catalytic cysteine residues, Cys88 and Cys378. When CaTHL is overexpressed in wild-type C. acetobutylicum, butanol production is reduced due to the disturbance of acidogenic to solventogenic shift. The CaTHL(V77Q/N153Y/A286K) mutant, which is not able to form disulfide bonds, exhibits higher activity than wild-type CaTHL, and enhances butanol production upon overexpression. On the basis of these results, we suggest that CaTHL functions as a key enzyme in the regulation of the main metabolism of C. acetobutylicum through a redox-switch regulatory mechanism.

PubMed: 26391388
DOI: 10.1038/ncomms9410

実験手法

X-RAY DIFFRACTION (2.1 Å)