4YVQ

Crystal Structure of FLU-TPR in Complex with the C-terminal Region of GluTR

Summary for 4YVQ

• Entry DOI: 10.2210/pdb4yvq/pdb
• Related: 4YVO
• Descriptor: Glutamyl-tRNA reductase 1, chloroplastic, Protein FLUORESCENT IN BLUE LIGHT, chloroplastic (3 entities in total)
• Functional Keywords: tpr, chloroplast, protein-protein interaction, oxidoreductase-fluorescent protein complex, oxidoreductase/fluorescent protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Cellular location: Plastid, chloroplast membrane : P42804; Plastid, chloroplast membrane; Single-pass membrane protein: Q940U6
• Total number of polymer chains: 2
• Total formula weight: 29913.37

Authors

Zhang, M.,Zhang, F.,Liu, L. (deposition date: 2015-03-20, release date: 2015-06-10, Last modification date: 2023-11-08)

Primary citation

Zhang, M.,Zhang, F.,Fang, Y.,Chen, X.,Chen, Y.,Zhang, W.,Dai, H.E.,Lin, R.,Liu, L.
The Non-canonical Tetratricopeptide Repeat (TPR) Domain of Fluorescent (FLU) Mediates Complex Formation with Glutamyl-tRNA Reductase.
J.Biol.Chem., 290:17559-17565, 2015

PubMed Abstract: The tetratricopeptide repeat (TPR)-containing protein FLU is a negative regulator of chlorophyll biosynthesis in plants. It directly interacts through its TPR domain with glutamyl-tRNA reductase (GluTR), the rate-limiting enzyme in the formation of δ-aminolevulinic acid (ALA). Delineation of how FLU binds to GluTR is important for understanding the molecular basis for FLU-mediated repression of synthesis of ALA, the universal tetrapyrrole precursor. Here, we characterize the FLU-GluTR interaction by solving the crystal structures of the uncomplexed TPR domain of FLU (FLU(TPR)) at 1.45-Å resolution and the complex of the dimeric domain of GluTR bound to FLU(TPR) at 2.4-Å resolution. Three non-canonical TPR motifs of each FLU(TPR) form a concave surface and clamp the helix bundle in the C-terminal dimeric domain of GluTR. We demonstrate that a 2:2 FLU(TPR)-GluTR complex is the functional unit for FLU-mediated GluTR regulation and suggest that the formation of the FLU-GluTR complex prevents glutamyl-tRNA, the GluTR substrate, from binding with this enzyme. These results also provide insights into the spatial regulation of ALA synthesis by the membrane-located FLU protein.

PubMed: 26037924
DOI: 10.1074/jbc.M115.662981

Experimental method

X-RAY DIFFRACTION (2.401 Å)