7CW5

Acetyl-CoA acetyltransferase from Bacillus cereus ATCC 14579

7CW5 の概要

• エントリーDOI: 10.2210/pdb7cw5/pdb
• 分子名称: Acetyl-CoA acetyltransferase, COENZYME A (3 entities in total)
• 機能のキーワード: acetyl-coa acetyltransferase, transferase
• 由来する生物種: Bacillus cereus ATCC 14579
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85990.64

構造登録者

Hong, J.,Kim, K.J. (登録日: 2020-08-27, 公開日: 2020-10-07, 最終更新日: 2023-11-29)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)