5LU4

C4-type pyruvate phosphate dikinase: conformational intermediate of central domain in the swiveling mechanism

Summary for 5LU4

• Entry DOI: 10.2210/pdb5lu4/pdb
• Descriptor: Pyruvate, phosphate dikinase, chloroplastic, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: phosphotransferase, nucleotide binding, conformational transition, swiveling mechanism, transferase
• Biological source: Flaveria trinervia (Clustered yellowtops)
• Cellular location: Plastid, chloroplast : P22221
• Total number of polymer chains: 2
• Total formula weight: 191737.59

Authors

Minges, A.,Hoeppner, A.,Groth, G. (deposition date: 2016-09-08, release date: 2017-05-24, Last modification date: 2024-01-17)

Primary citation

Minges, A.,Hoppner, A.,Groth, G.
Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism.
Protein Sci., 26:1667-1673, 2017

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

PubMed: 28470715
DOI: 10.1002/pro.3184

Experimental method

X-RAY DIFFRACTION (2.9 Å)