Structure of the acetophenone carboxylase core complex: prototype of a new class of ATP-dependent carboxylases/hydrolases.

ABSTRACT: Degradation of the aromatic ketone acetophenone is initiated by its carboxylation to benzoylacetate catalyzed by acetophenone carboxylase (Apc) in a reaction dependent on the hydrolysis of two ATP to ADP and P_i. Apc is a large protein complex which dissociates during purification into a heterooctameric Apc(αα'βγ)₂ core complex of 482 kDa and Apcε of 34 kDa. In this report, we present the X-ray structure of the Apc(αα'βγ)₂ core complex from Aromatoleum aromaticum at ca. 3 Å resolution which reveals a unique modular architecture and serves as model of a new enzyme family. Apcβ contains a novel domain fold composed of two β-sheets in a barrel-like arrangement running into a bundle of eight short polyproline (type II)-like helical segments. Apcα and Apcα' posse

SUBMITTER: Weidenweber S 

PROVIDER: S-EPMC5214803 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature