Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp

The atomic structure of the infectious, protease-resistant, β -sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β 2– α 2 loop of the bank vole prion pr...

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Published in:	Nature structural & molecular biology Vol. 25; no. 2; pp. 131 - 134
Main Authors:	Gallagher-Jones, Marcus, Glynn, Calina, Boyer, David R., Martynowycz, Michael W., Hernandez, Evelyn, Miao, Jennifer, Zee, Chih-Te, Novikova, Irina V., Goldschmidt, Lukasz, McFarlane, Heather T., Helguera, Gustavo F., Evans, James E., Sawaya, Michael R., Cascio, Duilio, Eisenberg, David S., Gonen, Tamir, Rodriguez, Jose A.
Format:	Journal Article
Language:	English
Published:	New York Nature Publishing Group US 01-02-2018 Nature Publishing Group
Subjects:	101/28 631/45/535/1258/1259 631/535/1266/1265 692/699 Amyloid - chemistry Amyloidogenic Proteins - chemistry Animals Atomic structure Banks (Finance) Biochemistry Biological Microscopy Biological research Biomedical and Life Sciences Bonds (Securities) Brief Communication Carbamazepine - chemistry Cattle Cricetinae Cryoelectron Microscopy Deer Electrons Fasteners Genomics Humans Hydrogen Hydrogen Bonding Hydrogen bonds Laboratories Life Sciences Membrane Biology Mice Molecular biology Nanocrystals Peptides Peptides - chemistry Phylogeny Physiological aspects Prion protein Prions (Proteins) Prions - chemistry Proteases Protein Structure Protein Structure, Secondary Proteins Proteome Proteomics Sheep Structure Surface Properties X-Ray Diffraction X-rays United States
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Abstract	The atomic structure of the infectious, protease-resistant, β -sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β 2– α 2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named ‘polar clasps’. MicroED structure of a peptide from the β2–α2 loop of the bank vole prion protein reveals a protofibril stabilized by a dense network of hydrogen bonds.
AbstractList	The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method, MicroED, we reveal the sub-1Å resolution structure of a protofibril formed by a wild-type segment from the β2-α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we name ‘polar clasps’. Ultrahigh-resolution cryo-EM structure reveals a prion protofibril stabilized by a dense three-dimensional network of hydrogen bonds. The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β2-α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named 'polar clasps'. The atomic structure of the infectious, protease-resistant, [beta]-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the [beta]2-[alpha]2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named 'polar clasps'. MicroED structure of a peptide from the [beta]2-[alpha]2 loop of the bank vole prion protein reveals a protofibril stabilized by a dense network of hydrogen bonds. The atomic structure of the infectious, protease-resistant, [beta]-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the [beta]2-[alpha]2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named 'polar clasps'. The atomic structure of the infectious, protease-resistant, β -sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β 2– α 2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named ‘polar clasps’. MicroED structure of a peptide from the β2–α2 loop of the bank vole prion protein reveals a protofibril stabilized by a dense network of hydrogen bonds.
Audience	Academic
Author	Cascio, Duilio Eisenberg, David S. Glynn, Calina Martynowycz, Michael W. Zee, Chih-Te Novikova, Irina V. Rodriguez, Jose A. Helguera, Gustavo F. Evans, James E. Goldschmidt, Lukasz Sawaya, Michael R. Boyer, David R. Hernandez, Evelyn Miao, Jennifer Gallagher-Jones, Marcus McFarlane, Heather T. Gonen, Tamir
AuthorAffiliation	1 Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA 4 Laboratory of Pharmaceutical Biotechnology, Institute of Biology and Experimental Medicine, Buenos Aires, AR 5 Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99354 2 Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles, Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, CA 90095, USA 3 Janelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, VA 20147, USA
AuthorAffiliation_xml	– name: 2 Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles, Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, CA 90095, USA – name: 4 Laboratory of Pharmaceutical Biotechnology, Institute of Biology and Experimental Medicine, Buenos Aires, AR – name: 5 Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99354 – name: 1 Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA – name: 3 Janelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, VA 20147, USA
Author_xml	– sequence: 1 givenname: Marcus surname: Gallagher-Jones fullname: Gallagher-Jones, Marcus organization: Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles – sequence: 2 givenname: Calina surname: Glynn fullname: Glynn, Calina organization: Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles – sequence: 3 givenname: David R. surname: Boyer fullname: Boyer, David R. organization: Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles, Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics – sequence: 4 givenname: Michael W. surname: Martynowycz fullname: Martynowycz, Michael W. organization: Janelia Research Campus, Howard Hughes Medical Institute – sequence: 5 givenname: Evelyn surname: Hernandez fullname: Hernandez, Evelyn organization: Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles – sequence: 6 givenname: Jennifer orcidid: 0000-0001-5527-295X surname: Miao fullname: Miao, Jennifer organization: Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles – sequence: 7 givenname: Chih-Te surname: Zee fullname: Zee, Chih-Te organization: Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles – sequence: 8 givenname: Irina V. surname: Novikova fullname: Novikova, Irina V. organization: Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory – sequence: 9 givenname: Lukasz surname: Goldschmidt fullname: Goldschmidt, Lukasz organization: Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles, Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics – sequence: 10 givenname: Heather T. surname: McFarlane fullname: McFarlane, Heather T. organization: Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles, Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics – sequence: 11 givenname: Gustavo F. surname: Helguera fullname: Helguera, Gustavo F. organization: Laboratory of Pharmaceutical Biotechnology, Institute of Biology and Experimental Medicine – sequence: 12 givenname: James E. surname: Evans fullname: Evans, James E. organization: Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory – sequence: 13 givenname: Michael R. surname: Sawaya fullname: Sawaya, Michael R. organization: Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles, Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics – sequence: 14 givenname: Duilio surname: Cascio fullname: Cascio, Duilio organization: Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles, Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics – sequence: 15 givenname: David S. orcidid: 0000-0003-2432-5419 surname: Eisenberg fullname: Eisenberg, David S. organization: Department of Biological Chemistry and Department of Chemistry and Biochemistry, University of California Los Angeles, Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics – sequence: 16 givenname: Tamir surname: Gonen fullname: Gonen, Tamir organization: Janelia Research Campus, Howard Hughes Medical Institute – sequence: 17 givenname: Jose A. orcidid: 0000-0001-8471-2504 surname: Rodriguez fullname: Rodriguez, Jose A. email: jrodriguez@mbi.ucla.edu organization: Department of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 NSFOTHERHHMI Author contributions: J.A.R. directed the work. J.A.R., J.M., E.H., M.W.M. and C.G. grew, evaluated and optimized crystals. J.A.R., D.R.B., C.G., M.R.S., H.T.M., M.G.J., C.Z., I.V.N, J.E.E. and D.C. collected data. J.A.R., C.G., J.M., M.G.J., M.R.S., D.C., M.W.M., G.H., E.H., L.G., D.S.E., and T.G. analyzed the data. C.G., M.G.J. and J.A.R. wrote the article, with input from all authors.
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Snippet	The atomic structure of the infectious, protease-resistant, β -sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we... The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we... The atomic structure of the infectious, protease-resistant, [beta]-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method... The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method, MicroED, we...
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SubjectTerms	101/28 631/45/535/1258/1259 631/535/1266/1265 692/699 Amyloid - chemistry Amyloidogenic Proteins - chemistry Animals Atomic structure Banks (Finance) Biochemistry Biological Microscopy Biological research Biomedical and Life Sciences Bonds (Securities) Brief Communication Carbamazepine - chemistry Cattle Cricetinae Cryoelectron Microscopy Deer Electrons Fasteners Genomics Humans Hydrogen Hydrogen Bonding Hydrogen bonds Laboratories Life Sciences Membrane Biology Mice Molecular biology Nanocrystals Peptides Peptides - chemistry Phylogeny Physiological aspects Prion protein Prions (Proteins) Prions - chemistry Proteases Protein Structure Protein Structure, Secondary Proteins Proteome Proteomics Sheep Structure Surface Properties X-Ray Diffraction X-rays
Title	Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp
URI	https://link.springer.com/article/10.1038/s41594-017-0018-0 https://www.ncbi.nlm.nih.gov/pubmed/29335561 https://www.proquest.com/docview/2188972257 https://search.proquest.com/docview/1989581391 https://www.osti.gov/biblio/1424794 https://pubmed.ncbi.nlm.nih.gov/PMC6170007
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