6bri

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==RHCC with unreduced and reduced Mercury complexes==
==RHCC with unreduced and reduced Mercury complexes==
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<StructureSection load='6bri' size='340' side='right' caption='[[6bri]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
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<StructureSection load='6bri' size='340' side='right'caption='[[6bri]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6bri]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Stamf Stamf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BRI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BRI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6bri]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylothermus_marinus_F1 Staphylothermus marinus F1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BRI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=HGI:MERCURY+(II)+IODIDE'>HGI</scene>, <scene name='pdbligand=HGN:mercuriomercury'>HGN</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.266&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Smar_1008 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=399550 STAMF])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=HGI:MERCURY+(II)+IODIDE'>HGI</scene>, <scene name='pdbligand=HGN:mercuriomercury'>HGN</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bri OCA], [https://pdbe.org/6bri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bri RCSB], [https://www.ebi.ac.uk/pdbsum/6bri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bri ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A3DN96_STAMF A3DN96_STAMF]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6bri" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Stamf]]
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[[Category: Large Structures]]
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[[Category: McDougall, M]]
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[[Category: Staphylothermus marinus F1]]
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[[Category: Stetefeld, J]]
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[[Category: McDougall M]]
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[[Category: Trieu, B]]
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[[Category: Stetefeld J]]
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[[Category: Archaea]]
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[[Category: Trieu B]]
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[[Category: Coiled-coil]]
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[[Category: Mercury]]
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[[Category: Metal binding protein]]
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[[Category: Nanoparticle]]
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[[Category: Nanotube]]
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RHCC with unreduced and reduced Mercury complexes

PDB ID 6bri

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