Structural intermediates and directionality of the swiveling motion of Pyruvate Phosphate Dikinase.

ABSTRACT: Pyruvate phosphate dikinase (PPDK) is a vital enzyme in cellular energy metabolism catalyzing the ATP- and P_i-dependent formation of phosphoenolpyruvate from pyruvate in C₄ -plants, but the reverse reaction forming ATP in bacteria and protozoa. The multi-domain enzyme is considered an efficient molecular machine that performs one of the largest single domain movements in proteins. However, a comprehensive understanding of the proposed swiveling domain motion has been limited by not knowing structural intermediates or molecular dynamics of the catalytic process. Here, we present crystal structures of PPDKs from Flaveria, a model genus for studying the evolution of C₄ -enzymes from phylogenetic ancestors. These structures resolve yet unknown conformational in

SUBMITTER: Minges A 

PROVIDER: S-EPMC5371819 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature