6BRI
RHCC with unreduced and reduced Mercury complexes
Summary for 6BRI
| Entry DOI | 10.2210/pdb6bri/pdb |
| Descriptor | Right Handed Coiled Coil, MERCURY (II) ION, IODIDE ION, ... (9 entities in total) |
| Functional Keywords | archaea, coiled-coil, nanotube, nanoparticle, mercury, metal binding protein |
| Biological source | Staphylothermus marinus F1 |
| Total number of polymer chains | 4 |
| Total formula weight | 27663.98 |
| Authors | McDougall, M.,Trieu, B.,Stetefeld, J. (deposition date: 2017-11-30, release date: 2018-02-07, Last modification date: 2023-10-04) |
| Primary citation | McDougall, M.,McEleney, K.,Francisco, O.,Trieu, B.,Ogbomo, E.K.,Tomy, G.,Stetefeld, J. Reductive power of the archaea right-handed coiled coil nanotube (RHCC-NT) and incorporation of mercury clusters inside protein cages. J. Struct. Biol., 203:281-287, 2018 Cited by PubMed Abstract: 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. PubMed: 29879486DOI: 10.1016/j.jsb.2018.05.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.266 Å) |
Structure validation
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