Metal site occupancy and allosteric switching in bacterial metal sensor proteins.

Metal site occupancy and allosteric switching in bacterial metal sensor proteins.
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细菌金属传感器蛋白中的金属位点占据和变构转换。

DOI:
10.1016/j.abb.2011.11.021
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发表时间:
2012-03-15
影响因子:
3.9
通讯作者:
Giedroc, David P.
Giedroc, David P.
中科院分区:
生物学3区
文献类型:
--
作者:
Guerra, Alfredo J.;Giedroc, David P.

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所有原核生物都编码一组金属传感器或金属调节蛋白,这些蛋白控制基因的表达,使生物体能够快速适应毒性或生物必需的过渡金属离子(例如锌、铜、铁和重金属污染物)的缺乏。因此,金属传感器蛋白可以被认为是细胞内过渡金属生物利用度的仲裁者,从而潜在地控制细胞中金属蛋白的金属化状态。金属传感器蛋白是一种特殊的变构蛋白,通过直接结合一个或两个同源金属离子来调节转录,从而排除所有其他金属离子。在大多数情况下,同源金属离子的结合会引起蛋白质寡聚物的结构变化,从而激活或抑制操纵基因 DNA 结合。特定金属驱动操纵基因 DNA 结合的金属调节程度的定量测量是变构耦合自由能 ΔGc。在这篇综述中,我们总结了最近的工作,旨在了解选定的金属传感器蛋白家族中这些变构开关的金属占据和金属选择性,并在功能背景下检查 ΔGc 的结构起源,即细胞内金属稳态的热力学“设定点”模型。
All prokaryotes encode a panel of metal sensor or metalloregulatory proteins that govern the expression of genes that allows an organism to quickly adapt to toxicity or deprivation of both biologically essential transition metal ions, e.g., Zn, Cu, Fe, and heavy metal pollutants. As such, metal sensor proteins can be considered arbiters of intracellular transition metal bioavailability and thus potentially control the metallation state of the metalloproteins in the cell. Metal sensor proteins are specialized allosteric proteins that regulate transcription as a result direct binding of one or two cognate metal ions, to the exclusion of all others. In most cases, the binding of the cognate metal ion induces a structural change in a protein oligomer that either activates or inhibits operator DNA binding. A quantitative measure of the degree to which a particular metal drives metalloregulation of operator DNA-binding is the allosteric coupling free energy, ΔGc. In this review, we summarize recent work directed toward understanding metal occupancy and metal selectivity of these allosteric switches in selected families of metal sensor proteins and examine the structural origins of ΔGc in the functional context a thermodynamic “set-point” model of intracellular metal homeostasis.
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