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首页> 外文期刊>Structure >A Self-Sequestered Calmodulin-like Ca~(~(~(2+))) Sensor of Mitochondrial SCaMC Carrier and Its Implication to Ca~(~(~(~(2+))))-Dependent ATP-Mg/Pi Transport
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A Self-Sequestered Calmodulin-like Ca~(~(~(2+))) Sensor of Mitochondrial SCaMC Carrier and Its Implication to Ca~(~(~(~(2+))))-Dependent ATP-Mg/Pi Transport

机译：线粒体SCaMC载体的自隔离钙调蛋白样Ca〜（〜（〜（2+）））传感器及其对Ca ~~~（〜（〜（〜（2+））））依赖性ATP-Mg / Pi的影响运输

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摘要

The mitochondrial carriers play essential roles in energy metabolism. The short Ca~(~(~(2+)))-binding mitochondrial carrier (SCaMC) transports ATP-Mg in exchange for Pi and is important for activities that depend on adenine nucleotides. SCaMC adopts, in addition to the transmembrane domain (TMD) that transports solutes, an extramembrane N-terminal domain (NTD) that regulates solute transport in a Ca~(~(~(2+)))-dependent manner. Crystal structure of the Ca~(~(~(2+)))-bound NTD reveals a compact architecture in which the functional EF hands are sequestered by an endogenous helical segment. Nuclear magnetic resonance (NMR) relaxation rates indicated that removal of Ca~(~(~(2+))) from NTD results in a major conformational switch from the rigid and compact Ca~(~(~(2+)))- bound state to the dynamic and loose apo state. Finally, we showed using surface plasmon resonance and NMR titration experiments that free apo NTDs could specifically interact with liposome-incorporated TMD, but that Ca~(~(~(2+))) binding drastically weakened the interaction. Our results together provide a molecular explanation for Ca~(~(~(2+)))-dependent ATP-Mg flux in mitochondria.
机译：线粒体载体在能量代谢中起重要作用。短的Ca〜（〜（〜（2+）））结合线粒体载体（SCaMC）转运ATP-Mg交换Pi，对于依赖腺嘌呤核苷酸的活性很重要。除转运溶质的跨膜结构域（TMD）外，SCaMC还采用以Ca〜（〜（〜（2（））））依赖的方式调节溶质转运的膜外N末端结构域（NTD）。 Ca〜（〜（〜（2+）））结合的NTD的晶体结构揭示了一个紧凑的体系结构，其中功能性EF手被内源性螺旋链段隔离。核磁共振（NMR）弛豫速率表明，从NTD中去除Ca〜（〜（〜（2 +）））-会导致刚性和致密Ca〜（〜（〜（2 +）））-的主要构象转换绑定状态变为动态和松散的载脂蛋白状态。最后，我们使用表面等离振子共振和NMR滴定实验表明，游离载脂蛋白NTD可以与掺入脂质体的TMD发生特异性相互作用，但Ca〜（〜（〜（2+）））结合会大大削弱相互作用。我们的研究结果共同为线粒体中Ca〜（〜（〜（2+）））依赖性ATP-Mg通量提供了分子解释。

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