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Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism
Author(s) -
Minges Alexander,
Höppner Astrid,
Groth Georg
Publication year - 2017
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3184
Subject(s) - phosphoenolpyruvate carboxykinase , chemistry , biophysics , catalytic cycle , mechanism (biology) , c4 photosynthesis , biochemistry , enzyme , function (biology) , atp synthase , biology , microbiology and biotechnology , physics , quantum mechanics
Pyruvate phosphate dikinase (PPDK) is an essential enzyme of both the C 4 photosynthetic pathway and cellular energy metabolism of some bacteria and unicellular protists. In C 4 plants, it catalyzes the ATP‐ and P i ‐dependent formation of phosphoenolpyruvate (PEP) while in bacteria and protozoa the ATP‐forming direction is used. PPDK is composed out of three distinct domains and exhibits one of the largest single domain movements known today during its catalytic cycle. However, little information about potential intermediate steps of this movement was available. A recent study resolved a discrete intermediate step of PPDK's swiveling movement, shedding light on the details of this intriguing mechanism. Here we present an additional structural intermediate that possibly represents another crucial step in the catalytic cycle of PPDK, providing means to get a more detailed understanding of PPDK's mode of function.