6g6c: Difference between revisions

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-'''Unreleased structure'''
-The entry 6g6c is ON HOLD
+==Crystal structure of a parallel six-helix coiled coil CC-Type2-LL-L17E==
+<StructureSection load='6g6c' size='340' side='right' caption='[[6g6c]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6g6c]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G6C FirstGlance]. <br>
+</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=6g6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g6c OCA], [http://pdbe.org/6g6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g6c RCSB], [http://www.ebi.ac.uk/pdbsum/6g6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g6c 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6g6c" 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]]