5hkr
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hkr OCA], [https://pdbe.org/5hkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hkr RCSB], [https://www.ebi.ac.uk/pdbsum/5hkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hkr ProSAT]</span></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=5hkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hkr OCA], [https://pdbe.org/5hkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hkr RCSB], [https://www.ebi.ac.uk/pdbsum/5hkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hkr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Learning to engineer self-assembly would enable the precise organization of molecules by design to create matter with tailored properties. Here we demonstrate that proteins can direct the self-assembly of buckminsterfullerene (C60) into ordered superstructures. A previously engineered tetrameric helical bundle binds C60 in solution, rendering it water soluble. Two tetramers associate with one C60, promoting further organization revealed in a 1.67-A crystal structure. Fullerene groups occupy periodic lattice sites, sandwiched between two Tyr residues from adjacent tetramers. Strikingly, the assembly exhibits high charge conductance, whereas both the protein-alone crystal and amorphous C60 are electrically insulating. The affinity of C60 for its crystal-binding site is estimated to be in the nanomolar range, with lattices of known protein crystals geometrically compatible with incorporating the motif. Taken together, these findings suggest a new means of organizing fullerene molecules into a rich variety of lattices to generate new properties by design. | ||
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| - | Protein-directed self-assembly of a fullerene crystal.,Kim KH, Ko DK, Kim YT, Kim NH, Paul J, Zhang SQ, Murray CB, Acharya R, DeGrado WF, Kim YH, Grigoryan G Nat Commun. 2016 Apr 26;7:11429. doi: 10.1038/ncomms11429. PMID:27113637<ref>PMID:27113637</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5hkr" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of de novo designed fullerene organising protein complex with fullerene
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