A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport.
A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport.
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DOI：
10.1016/j.str.2013.10.018
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发表时间：
2014-02-04
期刊：
影响因子：
5.7
通讯作者：
Chou, James J.
中科院分区：
文献类型：
--
作者：
Yang, Qin;Brueschweiler, Sven;Chou, James J.
The mitochondrial carriers play essential roles in energy metabolism. The short Ca2+-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 Ca2+-dependent manner. Crystal structure of the Ca2+-bound NTD reveals a compact architecture in which the functional EF hands are sequestered by an endogenous helical segment. NMR relaxation rates indicated that removal of Ca2+ from NTD results in a major conformational switch from the rigid and compact Ca2+-bound state to the dynamic and loose apo state. Finally, we showed using surface plasmon resonance and NMR titration experiments that free apo NTD could specifically interact with liposome-incorporated TMD, but Ca2+ binding drastically weakened the interaction. Our results together provide a molecular explanation for Ca2+-dependent ATP-Mg flux in mitochondria.
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