6bri
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6bri is ON HOLD Authors: Description: Category: Unreleased Structures) |
|||
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==RHCC with unreduced and reduced Mercury complexes== | |
| + | <StructureSection load='6bri' size='340' side='right'caption='[[6bri]], [[Resolution|resolution]] 3.27Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.266Å</td></tr> | ||
| + | <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> | ||
| + | <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> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A3DN96_STAMF A3DN96_STAMF] | ||
| + | <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> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6bri" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Staphylothermus marinus F1]] | ||
| + | [[Category: McDougall M]] | ||
| + | [[Category: Stetefeld J]] | ||
| + | [[Category: Trieu B]] | ||
Current revision
RHCC with unreduced and reduced Mercury complexes
| |||||||||||
