6bri
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bri OCA], [http://pdbe.org/6bri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bri RCSB], [http://www.ebi.ac.uk/pdbsum/6bri PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bri ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bri OCA], [http://pdbe.org/6bri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bri RCSB], [http://www.ebi.ac.uk/pdbsum/6bri PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bri ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
+ | |||
+ | Reductive power of the archaea right-handed coiled coil nanotube (RHCC-NT) and incorporation of mercury clusters inside protein cages.,McDougall M, McEleney K, Francisco O, Trieu B, Ogbomo EK, Tomy G, Stetefeld J J Struct Biol. 2018 Jun 5. pii: S1047-8477(18)30137-0. doi:, 10.1016/j.jsb.2018.05.013. PMID:29879486<ref>PMID:29879486</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6bri" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 06:23, 20 June 2018
RHCC with unreduced and reduced Mercury complexes
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Categories: Stamf | McDougall, M | Stetefeld, J | Trieu, B | Archaea | Coiled-coil | Mercury | Metal binding protein | Nanoparticle | Nanotube