Structural highlights
Publication Abstract from PubMed
Bacillus cereus ATCC 14579 is a known polyhydroxybutyrate (PHB)-producing microorganism that possesses genes associated with PHB synthesis such as PhaA, PhaB, and PHA synthases. PhaA (i.e., thiolase) is the first enzyme in the PHA biosynthetic pathway, which catalyze the condensation of two acetyl-CoA molecules to acetoacetyl-CoA. Our study elucidated the crystal structure of PhaA in Bacillus cereus ATCC 14579 (BcTHL) in its apo- and CoA-bound forms. BcTHL adopts a type II biosynthetic thiolase structure by forming a tetramer. The crystal structure of CoA-complexed BcTHL revealed that the substrate binding site of BcTHL is constituted by different residues compared with other known thiolases. Our study also revealed that Arg221, a residue involved in ADP binding, undergoes a positional conformational change upon the binding of the CoA molecule.
Crystal structure of an acetyl-CoA acetyltransferase from PHB producing bacterium Bacillus cereus ATCC 14579.,Hong J, Park W, Seo H, Kim IK, Kim KJ Biochem Biophys Res Commun. 2020 Sep 21. pii: S0006-291X(20)31789-7. doi:, 10.1016/j.bbrc.2020.09.048. PMID:32972748[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hong J, Park W, Seo H, Kim IK, Kim KJ. Crystal structure of an acetyl-CoA acetyltransferase from PHB producing bacterium Bacillus cereus ATCC 14579. Biochem Biophys Res Commun. 2020 Sep 21. pii: S0006-291X(20)31789-7. doi:, 10.1016/j.bbrc.2020.09.048. PMID:32972748 doi:http://dx.doi.org/10.1016/j.bbrc.2020.09.048
