Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution
Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution
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DOI：
10.1126/science.1127121
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发表时间：
2006-07-21
期刊：
影响因子：
56.9
通讯作者：
Nordlund, Par
中科院分区：
文献类型：
--
作者：
Eshaghi, Said;Niegowski, Damian;Nordlund, Par
CorA家族成员是广泛分布的二价金属离子转运蛋白，被认为是细菌和酵母的主要Mg 2+转运蛋白。我们已经确定了一个2.9埃的分辨率结构的CorA从海栖热袍菌，揭示了一个五聚体的锥形蛋白质。两个潜在的调节金属结合位点被发现在N-末端结构域，结合Mg 2+和Co 2+。CorA的结构支持涉及二价金属离子的脱水和再水化的外排系统，其可能由细胞质入口处的保守天冬氨酸残基环和孔周质侧的羰基漏斗介导。
CorA family members are ubiquitously distributed transporters of divalent metal cations and are considered to be the primary Mg2+ transporter of Bacteria and Archaea. We have determined a 2.9 angstrom resolution structure of CorA from Thermotoga maritima that reveals a pentameric cone shaped protein. Two potential regulatory metal binding sites are found in the N-terminal domain that bind both Mg2+ and Co2+. The structure of CorA supports an efflux system involving dehydration and rehydration of divalent metal ions potentially mediated by a ring of conserved aspartate residues at the cytoplasmic entrance and a carbonyl funnel at the periplasmic side of the pore.