6mk1
From Proteopedia
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</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=6mk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mk1 OCA], [http://pdbe.org/6mk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mk1 RCSB], [http://www.ebi.ac.uk/pdbsum/6mk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mk1 ProSAT]</span></td></tr> | </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=6mk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mk1 OCA], [http://pdbe.org/6mk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mk1 RCSB], [http://www.ebi.ac.uk/pdbsum/6mk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mk1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tandem repeat proteins exhibit native designability and represent potentially useful scaffolds for the construction of synthetic biomimetic assemblies. We have designed 2 synthetic peptides, HEAT_R1 and LRV_M3Delta1, based on the consensus sequences of single repeats of thermophilic HEAT (PBS_HEAT) and Leucine-Rich Variant (LRV) structural motifs, respectively. Self-assembly of the peptides afforded high-aspect ratio helical nanotubes. Cryo-electron microscopy with direct electron detection was employed to analyze the structures of the solvated filaments. The 3D reconstructions from the cryo-EM maps led to atomic models for the HEAT_R1 and LRV_M3Delta1 filaments at resolutions of 6.0 and 4.4 A, respectively. Surprisingly, despite sequence similarity at the lateral packing interface, HEAT_R1 and LRV_M3Delta1 filaments adopt the opposite helical hand and differ significantly in helical geometry, while retaining a local conformation similar to previously characterized repeat proteins of the same class. The differences in the 2 filaments could be rationalized on the basis of differences in cohesive interactions at the lateral and axial interfaces. These structural data reinforce previous observations regarding the structural plasticity of helical protein assemblies and the need for high-resolution structural analysis. Despite these observations, the native designability of tandem repeat proteins offers the opportunity to engineer novel helical nanotubes. Moreover, the resultant nanotubes have independently addressable and chemically distinguishable interior and exterior surfaces that would facilitate applications in selective recognition, transport, and release. | ||
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| + | Ambidextrous helical nanotubes from self-assembly of designed helical hairpin motifs.,Hughes SA, Wang F, Wang S, Kreutzberger MAB, Osinski T, Orlova A, Wall JS, Zuo X, Egelman EH, Conticello VP Proc Natl Acad Sci U S A. 2019 Jul 1. pii: 1903910116. doi:, 10.1073/pnas.1903910116. PMID:31262809<ref>PMID:31262809</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6mk1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:39, 13 November 2019
Cryo-EM of self-assembly peptide filament HEAT_R1
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