Minges, Alexander ORCID: 0000-0001-7760-2753, Hoeppner, Astrid ORCID: 0000-0002-7076-5936 and Groth, Georg (2017). Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism. Protein Sci., 26 (8). S. 1667 - 1674. HOBOKEN: WILEY. ISSN 1469-896X

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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.

Item Type: Journal Article
CreatorsEmailORCIDORCID Put Code
Minges, AlexanderUNSPECIFIEDorcid.org/0000-0001-7760-2753UNSPECIFIED
Hoeppner, AstridUNSPECIFIEDorcid.org/0000-0002-7076-5936UNSPECIFIED
URN: urn:nbn:de:hbz:38-223461
DOI: 10.1002/pro.3184
Journal or Publication Title: Protein Sci.
Volume: 26
Number: 8
Page Range: S. 1667 - 1674
Date: 2017
Publisher: WILEY
Place of Publication: HOBOKEN
ISSN: 1469-896X
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
ROTATION; SYSTEMMultiple languages
Biochemistry & Molecular BiologyMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/22346


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