6g6e
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a parallel seven-helix coiled coil CC-Type2-deLI== | |
| + | <StructureSection load='6g6e' size='340' side='right'caption='[[6g6e]], [[Resolution|resolution]] 1.26Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6g6e]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G6E 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]] 1.26Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EO2:(2~{S})-2-azanyl-4-methyl-pent-4-enoic+acid'>EO2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[https://proteopedia.org/fgij/fg.htm?mol=6g6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g6e OCA], [https://pdbe.org/6g6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g6e RCSB], [https://www.ebi.ac.uk/pdbsum/6g6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g6e 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 6g6e" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Brady RL]] | ||
| + | [[Category: Rhys GG]] | ||
| + | [[Category: Woolfson DN]] | ||
Current revision
Crystal structure of a parallel seven-helix coiled coil CC-Type2-deLI
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