5XN6

Heterodimer crystal structure of geranylgeranyl diphosphate synthases 1 with GGPPS Recruiting Protein(OsGRP) from Oryza sativa

5XN6 の概要

• エントリーDOI: 10.2210/pdb5xn6/pdb
• 分子名称: Os07g0580900 protein, Os02g0668100 protein (2 entities in total)
• 機能のキーワード: heterodimer, small-subunit, transferase, osggpps1, osgrp
• 由来する生物種: Oryza sativa Japonica Group (Rice); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 194979.68

構造登録者

Wang, C.,Zhou, F.,Lu, S.,Zhang, P. (登録日: 2017-05-18, 公開日: 2017-06-28, 最終更新日: 2023-11-22)

主引用文献

Zhou, F.,Wang, C.Y.,Gutensohn, M.,Jiang, L.,Zhang, P.,Zhang, D.,Dudareva, N.,Lu, S.
A recruiting protein of geranylgeranyl diphosphate synthase controls metabolic flux toward chlorophyll biosynthesis in rice
Proc. Natl. Acad. Sci. U.S.A., 114:6866-6871, 2017

PubMed Abstract: In plants, geranylgeranyl diphosphate (GGPP) is produced by plastidic GGPP synthase (GGPPS) and serves as a precursor for vital metabolic branches, including chlorophyll, carotenoid, and gibberellin biosynthesis. However, molecular mechanisms regulating GGPP allocation among these biosynthetic pathways localized in the same subcellular compartment are largely unknown. We found that rice contains only one functionally active GGPPS, OsGGPPS1, in chloroplasts. A functionally active homodimeric enzyme composed of two OsGGPPS1 subunits is located in the stroma. In thylakoid membranes, however, the GGPPS activity resides in a heterodimeric enzyme composed of one OsGGPPS1 subunit and GGPPS recruiting protein (OsGRP). OsGRP is structurally most similar to members of the geranyl diphosphate synthase small subunit type II subfamily. In contrast to members of this subfamily, OsGRP enhances OsGGPPS1 catalytic efficiency and specificity of GGPP production on interaction with OsGGPPS1. Structural biology and protein interaction analyses demonstrate that affinity between OsGRP and OsGGPPS1 is stronger than between two OsGGPPS1 molecules in homodimers. OsGRP determines OsGGPPS1 suborganellar localization and directs it to a large protein complex in thylakoid membranes, consisting of geranylgeranyl reductase (OsGGR), light-harvesting-like protein 3 (OsLIL3), protochlorophyllide oxidoreductase (OsPORB), and chlorophyll synthase (OsCHLG). Taken together, genetic and biochemical analyses suggest OsGRP functions in recruiting OsGGPPS1 from the stroma toward thylakoid membranes, thus providing a mechanism to control GGPP flux toward chlorophyll biosynthesis.

PubMed: 28607067
DOI: 10.1073/pnas.1705689114

実験手法

X-RAY DIFFRACTION (3.598 Å)