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:EN
Published: Nature Portfolio 2017
Subjects:
R
Q
Online Access:https://doaj.org/article/5148c7bfd75e4a51860c3bbe2fa28754
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