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Protein Sci. 2017 Aug;26(8):1667-1673. doi: 10.1002/pro.3184. Epub 2017 May 12.

Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism.

Author information

1
Cluster of Excellence on Plant Sciences (CEPLAS), Institute of Biochemical Plant Physiology, Heinrich Heine University Düsseldorf, Düsseldorf, 40204, Germany.
2
X-ray Facility and Crystal Farm, Heinrich Heine University Düsseldorf, Düsseldorf, 40204, Germany.

Abstract

Pyruvate phosphate dikinase (PPDK) is an essential enzyme of both the C4 photosynthetic pathway and cellular energy metabolism of some bacteria and unicellular protists. In C4 plants, it catalyzes the ATP- and Pi -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.

KEYWORDS:

C4 photosynthesis; catalytic intermediate; pyruvate phosphate dikinase; swiveling domain mechanism

PMID:
28470715
DOI:
10.1002/pro.3184
[Indexed for MEDLINE]
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