4YVO
Crystal Structure of the TPR Domain of Arabidopsis FLU (FLU-TPR)
Summary for 4YVO
| Entry DOI | 10.2210/pdb4yvo/pdb |
| Related | 4YVQ |
| Descriptor | Protein FLUORESCENT IN BLUE LIGHT, chloroplastic (2 entities in total) |
| Functional Keywords | tpr, chloroplast, fluorescent protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Plastid, chloroplast membrane; Single-pass membrane protein: Q940U6 |
| Total number of polymer chains | 1 |
| Total formula weight | 18425.98 |
| Authors | |
| 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 Cited by 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: 26037924DOI: 10.1074/jbc.M115.662981 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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