Summary for 4XL4
| Entry DOI | 10.2210/pdb4xl4/pdb |
| Related | 4XL2 4XL3 |
| Descriptor | Acetyl-CoA acetyltransferase, COENZYME A, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | Clostridium acetobutylicum (strain EA 2018) |
| Total number of polymer chains | 2 |
| Total formula weight | 86870.72 |
| Authors | |
| Primary citation | 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 Cited by 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: 26391388DOI: 10.1038/ncomms9410 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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