{"reference": "Nat Commun. 2018 Aug 29;9(1):3512.", "alternative_name": "", "entry": "S-0542", "gene_names": "", "remarks": "Crystal Structure of the Amyloid-like, out-of-register beta-sheets, polymorph of the LFKFFK segment from the S. aureus PSMalpha3", "secondary_structure": "LFKFFK#CCEEEC&LFKFFK#CCEEEC", "chain_id": "A%%B%%B", "inchi": "InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2%%InChI=1S/Na/q+1%%InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2", "amyloid_non_amyloid": "Non-amyloid", "pmid": "30158633", "ligand_smiles": "[O-]S(=O)(=O)[O-]%%[Na+]%%[O-]S(=O)(=O)[O-]", "keyword": "Psm alpha-3", "peptide_protein_sequence": "chain-ID A: LFKFFK; chain-ID B: LFKFFK", "uniprot_ac": "H9BRQ7", "protein_name": "Psm alpha-3", "r_value_free": "0.187", "mutation_s_field": "No", "ligand_mw": "96.06%%22.99%%96.06", "pdb_id": "6FHD", "inchi_key": "QAOWNCQODCNURD-UHFFFAOYSA-L%%FKNQFGJONOIPTF-UHFFFAOYSA-N%%QAOWNCQODCNURD-UHFFFAOYSA-L", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "type": "Fibril", "author": "Salinas, N., Colletier, J.P., Moshe, A., Landau, M.", "species": "Staphylococcus aureus", "ligand_id": "SO4%%nan%%SO4", "method": "X-RAY DIFFRACTION", "ligand_name": "SULFATE ION%%SODIUM ION%%SULFATE ION", "global_stoichiometry": "Homo 36-mer - A36", "resolution": "1.85", "ligand_formula": "O4 S -2%%Na 1%%O4 S -2", "length": "6", "ligstr": "SO4:A:O4 S -2:96.06:SULFATE ION:[O-]S(=O)(=O)[O-]:InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2:QAOWNCQODCNURD-UHFFFAOYSA-L;nan:B:Na 1:22.99:SODIUM ION:[Na+]:InChI=1S/Na/q+1:FKNQFGJONOIPTF-UHFFFAOYSA-N;SO4:B:O4 S -2:96.06:SULFATE ION:[O-]S(=O)(=O)[O-]:InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2:QAOWNCQODCNURD-UHFFFAOYSA-L", "description": "They show that PSMAlpha1 and PSMAlpha4, involved in biofilm structuring, form canonical cross-Beta amyloid fibrils wherein Beta-sheets tightly mate through steric zipper interfaces, conferring high stability. Contrastingly, a truncated PSMAlpha3 has antibacterial activity, forms reversible fibrils, and reveals two polymorphic and atypical Beta-rich fibril architectures. These architectures are radically different from both the cross-Alpha fibrils formed by full-length PSMAlpha3, and from the canonical cross-Beta fibrils."}