5Y78
Crystal structure of the triose-phosphate/phosphate translocator in complex with inorganic phosphate
5Y78 の概要
| エントリーDOI | 10.2210/pdb5y78/pdb |
| 分子名称 | Putative hexose phosphate translocator, PHOSPHATE ION, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total) |
| 機能のキーワード | chloroplast, inner envelop membrane, antiporter, sugar phosphate, transport protein |
| 由来する生物種 | Galdieria sulphuraria (Red alga) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 88315.01 |
| 構造登録者 | Lee, Y.,Nishizawa, T.,Takemoto, M.,Kumazaki, K.,Yamashita, K.,Hirata, K.,Minoda, A.,Nagatoishi, S.,Tsumoto, K.,Ishitani, R.,Nureki, O. (登録日: 2017-08-16, 公開日: 2017-10-04, 最終更新日: 2023-11-22) |
| 主引用文献 | Lee, Y.,Nishizawa, T.,Takemoto, M.,Kumazaki, K.,Yamashita, K.,Hirata, K.,Minoda, A.,Nagatoishi, S.,Tsumoto, K.,Ishitani, R.,Nureki, O. Structure of the triose-phosphate/phosphate translocator reveals the basis of substrate specificity Nat Plants, 3:825-832, 2017 Cited by PubMed Abstract: The triose-phosphate/phosphate translocator (TPT) catalyses the strict 1:1 exchange of triose-phosphate, 3-phosphoglycerate and inorganic phosphate across the chloroplast envelope, and plays crucial roles in photosynthesis. Despite rigorous study for more than 40 years, the molecular mechanism of TPT is poorly understood because of the lack of structural information. Here we report crystal structures of TPT bound to two different substrates, 3-phosphoglycerate and inorganic phosphate, in occluded conformations. The structures reveal that TPT adopts a 10-transmembrane drug/metabolite transporter fold. Both substrates are bound within the same central pocket, where conserved lysine, arginine and tyrosine residues recognize the shared phosphate group. A structural comparison with the outward-open conformation of the bacterial drug/metabolite transporter suggests a rocker-switch motion of helix bundles, and molecular dynamics simulations support a model in which this rocker-switch motion is tightly coupled to the substrate binding, to ensure strict 1:1 exchange. These results reveal the unique mechanism of sugar phosphate/phosphate exchange by TPT. PubMed: 28970497DOI: 10.1038/s41477-017-0022-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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