Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 203, Issue 3, Pages 281-287Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2018.05.013
Keywords
Archaea; S-layer; Right-handed coiled coil; Reduction of metals; Cluster uptake via protein cage; Synchrotron-XRD; XPS
Funding
- Natural Science and Engineering Council of Canada [RGPIN 342077-2012, RGPIN-004954-2017, STGP 479210-2015]
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Coiled 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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