Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein

@article{Zhao2014CrystalSO,
  title={Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein},
  author={Aiguo Zhao and Ying Fang and X. Chen and Shun Zhao and W. Dong and Y. Lin and W. Gong and L. Liu},
  journal={Proceedings of the National Academy of Sciences},
  year={2014},
  volume={111},
  pages={6630 - 6635}
}
Significance The glutamyl-tRNA reductase (GluTR)-catalyzed reduction of glutamyl-tRNA is the rate-limiting and a pivotal regulation step in the tetrapyrrole biosynthetic pathway. In chloroplast-containing photosynthetic organisms, GluTR binding protein (GluBP) is a newly identified spatial regulator that allocates GluTR for synthesis of different tetrapyrrole products. We find that GluBP stimulates GluTR catalytic efficiency. The structure of the GluTR–GluBP complex shows that GluBP binding… Expand
33 Citations
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The Non-canonical Tetratricopeptide Repeat (TPR) Domain of Fluorescent (FLU) Mediates Complex Formation with Glutamyl-tRNA Reductase*
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