View source for 6g65


==Crystal structure of a parallel six-helix coiled coil CC-Type2-VV==
<StructureSection load='6g65' size='340' side='right'caption='[[6g65]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6g65]] is a 12 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=6G65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G65 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]] 1.15&#8491;</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=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=6g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g65 OCA], [https://pdbe.org/6g65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g65 RCSB], [https://www.ebi.ac.uk/pdbsum/6g65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g65 ProSAT]</span></td></tr>
</table>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6g65" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Brady RL]]
[[Category: Rhys GG]]
[[Category: Woolfson DN]]