Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump.

Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump.
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DOI:
10.1371/journal.pone.0015610
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发表时间:
2011-01-07
期刊:
影响因子:
3.7
通讯作者:
van den Berg B
van den Berg B
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Kulathila R;Kulathila R;Indic M;van den Berg B

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虽然铜具有作为酶辅助因子的基本功能,但过量的铜离子对细胞是有毒的,需要调节其水平的机制。大肠杆菌的CusCBFA操纵子编码一个四组分的外排泵,专门用于铜(I)和银(I)离子的挤出。我们已经解决了CUS重金属外排泵外膜组件CusC的X射线晶体结构,分辨率为2.3?该结构在所有外膜因子(OMF)蛋白中具有最大的细胞外开放,并首次表明存在一个三酰化的N-末端脂质锚。CusC蛋白没有任何明显的特征使其对金属离子具有特异性,这表明泵的窄底物特异性是由泵的其他组件提供的,最有可能是由内膜组件CUSA提供的。
While copper has essential functions as an enzymatic co-factor, excess copper ions are toxic for cells, necessitating mechanisms for regulating its levels. The cusCBFA operon of E. coli encodes a four-component efflux pump dedicated to the extrusion of Cu(I) and Ag(I) ions. We have solved the X-ray crystal structure of CusC, the outer membrane component of the Cus heavy metal efflux pump, to 2.3 Å resolution. The structure has the largest extracellular opening of any outer membrane factor (OMF) protein and suggests, for the first time, the presence of a tri-acylated N-terminal lipid anchor. The CusC protein does not have any obvious features that would make it specific for metal ions, suggesting that the narrow substrate specificity of the pump is provided by other components of the pump, most likely by the inner membrane component CusA.
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