Xue Yi, Davis Anna V, Balakrishnan Gurusamy, Stasser Jay P, Staehlin Benjamin M, Focia Pamela, Spiro Thomas G, Penner-Hahn James E, O'Halloran Thomas V
Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.
Nat Chem Biol. 2008 Feb;4(2):107-9. doi: 10.1038/nchembio.2007.57. Epub 2007 Dec 23.
Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.
富含甲硫氨酸的基序在包括CusF蛋白在内的铜转运因子中发挥着重要作用。在此我们表明,CusF利用了一个新的金属识别位点,其中Cu(I)从一个Met2His配体平面沿四方方向朝着一个保守的色氨酸位移。光谱研究表明,硫醚配位以及与色氨酸的强阳离子-π相互作用均能稳定金属结合。这种新型活性位点化学为控制偶然金属的氧化还原和取代化学提供了机制。