5LU4

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

5LU4 の概要

• エントリーDOI: 10.2210/pdb5lu4/pdb
• 分子名称: Pyruvate, phosphate dikinase, chloroplastic, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: phosphotransferase, nucleotide binding, conformational transition, swiveling mechanism, transferase
• 由来する生物種: Flaveria trinervia (Clustered yellowtops)
• 細胞内の位置: Plastid, chloroplast : P22221
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 191737.59

構造登録者

Minges, A.,Hoeppner, A.,Groth, G. (登録日: 2016-09-08, 公開日: 2017-05-24, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)