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標題: 科學家闡述AdiC轉運機理 [打印本頁]

作者: ccarter0329    時間: 2011-2-27 11:18     標題: 科學家闡述AdiC轉運機理

清華大學生命科學學院施一公教授領導的研究組在《自然》在線發表論文,闡述在毒性大腸桿菌腸胃耐酸性保護機制中起重要作用的AdiC轉運蛋白的底物識別和轉運機理。這是繼他們在2009年於《科學》發表首個APC家族轉運蛋白晶體結構之後針對AdiC研究的又一重要突破。

AdiC是逆向轉運arginine及其脫羧產物agmatine的轉運蛋白。2009年5月,施一公教授的研究組發表了AdiC在沒有底物狀況下的3.6埃的分子結構,揭示了AdiC以二聚體形式存在,同時還發現APC家族的轉運蛋白與其他幾類沒有序列同源性的鈉離子依賴性轉運蛋白具有相似的結構骨架。根據生化實驗結果,他們推測出在轉運過程中起重要作用的氨基酸殘基以及可能的轉運模型。

在《自然》最新發表的論文中,施一公研究組解析了AdiC在arginine結合狀態下的3.0埃的晶體結構。這個較高分辨率的結構顯示,過去報道的AdiC由於分辨率偏低、數據質量有限,因而儘管基本結論正確,但在部分跨膜螺旋區域,施一公的研究組以及美國另一研究組均存在結構修正不妥之處。所以在這一篇文章裡,他們首先糾正了兩個組以前的偏差,然後比較了AdiC在沒有底物和結合arginine的狀態下的結構。這一比較顯示,在結合arginine時,AdiC的跨膜螺旋TM6旋轉了近40°,覆蓋於底物之上,使底物處於一個完全封閉的表面呈負電勢的腔中。在這一觀測的基礎上,結合以往的生化數據,他們進一步修正了AdiC的轉運模型,提出了逆向轉運蛋白雙結合位點的模型。
作者: uyk80x0z    時間: 2017-11-25 22:10     標題: yeti tumbler Xu | Forum

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