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6g67
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a parallel eight-helix coiled coil CC-Type2-II== | |
| + | <StructureSection load='6g67' size='340' side='right' caption='[[6g67]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6g67]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G67 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=6g67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g67 OCA], [http://pdbe.org/6g67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g67 RCSB], [http://www.ebi.ac.uk/pdbsum/6g67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g67 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In coiled-coil (CC) protein structures alpha-helices wrap around one another to form rope-like assemblies. Most natural and designed CCs have two-four helices and cyclic (Cn) or dihedral (Dn) symmetry. Increasingly, CCs with five or more helices are being reported. A subset of these higher-order CCs is of interest as they have accessible central channels that can be functionalised; they are alpha-helical barrels. These extended cavities are surprising given the drive to maximise buried hydrophobic surfaces during protein folding and assembly in water. Here, we show that alpha-helical barrels can be maintained by the strategic placement of beta-branched aliphatic residues lining the lumen. Otherwise, the structures collapse or adjust to give more-complex multi-helix assemblies without Cn or Dn symmetry. Nonetheless, the structural hallmark of CCs-namely, knobs-into-holes packing of side chains between helices-is maintained leading to classes of CCs hitherto unobserved in nature or accessed by design. | ||
| - | + | Maintaining and breaking symmetry in homomeric coiled-coil assemblies.,Rhys GG, Wood CW, Lang EJM, Mulholland AJ, Brady RL, Thomson AR, Woolfson DN Nat Commun. 2018 Oct 8;9(1):4132. doi: 10.1038/s41467-018-06391-y. PMID:30297707<ref>PMID:30297707</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6g67" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Brady, R L]] | ||
| + | [[Category: Rhys, G G]] | ||
| + | [[Category: Woolfson, D N]] | ||
| + | [[Category: Alpha-helical bundle]] | ||
| + | [[Category: Coiled coil]] | ||
| + | [[Category: De novo]] | ||
| + | [[Category: De novo protein]] | ||
| + | [[Category: Synthetic construct]] | ||
Current revision
Crystal structure of a parallel eight-helix coiled coil CC-Type2-II
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