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The binding mode of Ni-(L-His)2 in NikA revealed by X-ray crystallography.

J. Inorg. Biochem.2013 Apr;121:16-8. Epub 2012 Dec 23
Hugo Lebrette 1 , Marina Iannello , Juan C Fontecilla-Camps , Christine Cavazza
Hugo Lebrette 1 , Marina Iannello , Juan C Fontecilla-Camps , Christine Cavazza

[No authors listed]

Author information
  • 1 Institut de Biologie Structurale Jean-Pierre Ebel, Metalloproteins Group, UMR 5075, CEA, CNRS, Université Joseph Fourier-Grenoble 1, 41, rue Jules Horowitz 38027 Grenoble Cedex 1, France.

摘要


The ABC-type importer NikABCDE mediates nickel acquisition in Escherichia coli. The periplasmic nickel-binding component NikA has a folding similar to that of the peptide transporter OppA and does not bind free nickel. Instead, we showed that the metal is tetra-coordinated by an organic tri-dentate molecule and His416. Conversely, it has been recently reported that NikA binds Ni-(L-His)2 and that addition of histidine increases the rate of nickel uptake in vivo. Here, we report the structure of NikA/Ni-(L-His)2 and show that histidine binding differs from peptide binding in OppA. The structure also confirms the central role of His416 in nickel binding.