5CHE

Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its regulatory proteins

Summary for 5CHE

• Entry DOI: 10.2210/pdb5che/pdb
• Descriptor: Glutamyl-tRNA reductase 1, chloroplastic, Glutamyl-tRNA reductase-binding protein, chloroplastic, Protein FLUORESCENT IN BLUE LIGHT, chloroplastic, ... (4 entities in total)
• Functional Keywords: glutr, tertiary complex, regulatory proteins, anchor protein, oxidoreductase
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Cellular location: Plastid, chloroplast membrane : P42804; Plastid, chloroplast stroma : Q9LU39; Plastid, chloroplast membrane ; Single-pass membrane protein: Q940U6
• Total number of polymer chains: 6
• Total formula weight: 208367.63

Authors

Fang, Y.,Liu, L. (deposition date: 2015-07-10, release date: 2016-02-03, Last modification date: 2023-11-08)

Primary citation

Fang, Y.,Zhao, S.,Zhang, F.,Zhao, A.,Zhang, W.,Zhang, M.,Liu, L.
The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein
Sci Rep, 6:19756-19756, 2016

PubMed Abstract: Tetrapyrrole biosynthesis is an essential and tightly regulated process, and glutamyl-tRNA reductase (GluTR) is a key target for multiple regulatory factors at the post-translational level. By binding to the thylakoid membrane protein FLUORESCENT (FLU) or the soluble stromal GluTR-binding protein (GBP), the activity of GluTR is down- or up-regulated. Here, we reconstructed a ternary complex composed of the C-terminal tetratricopepetide-repeat domain of FLU, GBP, and GluTR, crystallized and solved the structure of the complex at 3.2 Å. The overall structure resembles the shape of merged two binary complexes as previously reported, and shows a large conformational change within GluTR. We also demonstrated that GluTR binds tightly with GBP but does not bind to GSAM under the same condition. These findings allow us to suggest a biological role of the ternary complex for the regulation of plant GluTR.

PubMed: 26794057
DOI: 10.1038/srep19756

Experimental method

X-RAY DIFFRACTION (3.203 Å)