7CW4

Acetyl-CoA acetyltransferase from Bacillus cereus ATCC 14579

Summary for 7CW4

• Entry DOI: 10.2210/pdb7cw4/pdb
• Descriptor: Acetyl-CoA acetyltransferase, GLYCEROL (3 entities in total)
• Functional Keywords: acetyl-coa acetyltransferase, transferase
• Biological source: Bacillus cereus ATCC 14579
• Total number of polymer chains: 2
• Total formula weight: 84731.85

Authors

Hong, J.,Kim, K.J. (deposition date: 2020-08-27, release date: 2020-10-07, Last modification date: 2023-11-29)

Primary citation

Hong, J.,Park, W.,Seo, H.,Kim, I.K.,Kim, K.J.
Crystal structure of an acetyl-CoA acetyltransferase from PHB producing bacterium Bacillus cereus ATCC 14579.
Biochem.Biophys.Res.Commun., 533:442-448, 2020

PubMed Abstract: 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.

PubMed: 32972748
DOI: 10.1016/j.bbrc.2020.09.048

Experimental method

X-RAY DIFFRACTION (1.56 Å)