On the potential alternate binding change mechanism in a dimeric structure of Pyruvate Phosphate Dikinase

Abstract The pyruvate phosphate dikinase (PPDK) reaction mechanism is characterized by a distinct spatial separation of reaction centers and large conformational changes involving an opening-closing motion of the nucleotide-binding domain (NBD) and a swiveling motion of the central domain (CD). Howe...

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Bibliographic Details
Main Authors: Daniel Ciupka, Holger Gohlke
Format: Article
Language:English
Published: Nature Publishing Group 2017-08-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-017-08521-w