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真核生物磷酸鹽轉運蛋白的晶體結構
研究人員報告了一個真菌高親和性磷酸鹽轉運蛋白PiPT在磷酸鹽存在時的X-射線晶體結構，它處在一種朝向里面的、被阻隔的狀態。該結構可以解釋該轉運蛋白對于磷酸鹽親和性和結合特異性的機制，并將質子動力與磷酸鹽轉位了起來。
PiPT磷酸轉運蛋白的晶體結構為那些與癌癥和糖尿病等疾病有關的關鍵轉運蛋白等提供了一個有用模型。
Crystal structure of a eukaryotic phosphate transporter
Bjørn P. Pedersen, Hemant Kumar, Andrew B. Waight, Aaron J. Risenmay, Zygy Roe-Zurz,Bryant H. Chau, Avner Schlessinger, Massimiliano Bonomi, William Harries, Andrej Sali,Atul K. Johri & Robert M. Stroud
Phosphate is crucial for structural and metabolic needs, including nucleotide and lipid synthesis, signalling and chemical energy storage. Proton-coupled transporters of the major facilitator superfamily （MFS） are essential for phosphate uptake in plants and fungi, and also have a function in sensing external phosphate levels as transceptors1, 2, 3, 4, 5. Here we report the 2.9 Å structure of a fungal （Piriformospora indica） high-affinity phosphate transporter, PiPT, in an inward-facing occluded state,
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