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000418925 1001_ $$aMcDougall, Matthew$$b0
000418925 245__ $$aReductive power of the archaea right-handed coiled coil nanotube (RHCC-NT) and incorporation of mercury clusters inside protein cages
000418925 260__ $$aSan Diego, Calif.$$bElsevier$$c2018
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000418925 520__ $$aCoiled coils are well described as powerful oligomerization motifs and exhibit a large diversity of functions, including gene regulation, cell division, membrane fusion and drug extrusion. The archaea S-layer originated right-handed coiled coil –RHCC-NT- is characterized by extreme stability and is free of cysteine and histidine moieties. In the current study, we have followed a multidisciplinary approach to investigate the capacity of RHCC-NT to bind a variety of ionic complex metal ions. At the outside of the RHCC-NT, one mercury ion forms an electrostatic interaction with the S-methyl moiety of the single methionine residue present in each coil. We demonstrate that RHCC-NT is reducing and incorporating metallic mercury in the large-sized interior cavities which are lined up along the tetrameric channel.
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000418925 7001_ $$aMcEleney, Kevin$$b1
000418925 7001_ $$aFrancisco, Olga$$b2
000418925 7001_ $$aTrieu, Benchmen$$b3
000418925 7001_ $$aOgbomo, Efehi Kelly$$b4
000418925 7001_ $$aTomy, Gregg$$b5
000418925 7001_ $$0P:(DE-HGF)0$$aStetefeld, Jörg$$b6$$eCorresponding author
000418925 773__ $$0PERI:(DE-600)1469822-5$$a10.1016/j.jsb.2018.05.013$$gVol. 203, no. 3, p. 281 - 287$$n3$$p281 - 287$$tJournal of structural biology$$v203$$x1047-8477$$y2018
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