{"method": "X-RAY DIFFRACTION", "mutation_s_field": "No", "ec_number": "", "description": "For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which the atomic structure of the cross-Beta spine is determined. It is a double Beta-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.", "ligstr": "", "pmid": "15944695", "remarks": "Structure of GNNQQNY from yeast prion Sup35; Structure of the cross-beta spine", "amyloid_non_amyloid": "Amyloid", "type": "Fibril", "inchi": "", "resolution": "1.8", "species": "Saccharomyces cerevisiae", "secondary_structure": "GNNQQNY#CCCCCCC", "chain_id": "", "gene_names": "", "r_value_free": "0.19", "pdb_id": "1YJP", "reference": "Nature. 2005 Jun 9;435(7043):773-8", "keyword": "Eukaryotic peptide chain release factor GTP-binding subunit", "protein_name": "Eukaryotic peptide chain release factor GTP-binding subunit", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: GNNQQNY", "entry": "S-0076", "length": "7", "uniprot_ac": "P05453", "author": "Nelson, R., Sawaya, M.R., Balbirnie, M., Madsen, A.O., Riekel, C., Grothe, R., Eisenberg, D.", "ligand_smiles": "", "ligand_mw": "", "alternative_name": "", "ligand_name": "", "pdb_classification": "PROTEIN BINDING", "global_stoichiometry": "Homo 2-mer - A2 ", "inchi_key": "", "ligand_id": ""}