{"method": "SOLUTION NMR", "mutation_s_field": "No", "ec_number": "", "description": "In vitro, MPG1 assembles spontaneously into amyloid structures. The assembly of MPG1 only occurs at a hydrophobic:hydrophilic interface and can be modulated by MHP1 and other factors. They further show that MPG1 assemblies can much more effectively retain cutinase 2 activity on a surface after co-incubation and extensive washing compared with other protein coatings. The assembly and interactions of MPG1 at hydrophobic surfaces thereby provide the basis for a possible mechanism by which the fungus can develop appropriately at the infection interface.", "ligstr": "", "pmid": "27142249", "remarks": "Solution structure of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae", "amyloid_non_amyloid": "Amyloid", "type": "Protein", "inchi": "", "resolution": "", "species": "Pyricularia oryzae", "secondary_structure": "SAIPAPGEGPSVSMAQQKCGAEKVVSCCNSKELKNSKSGAEIPIDVLSGECKNIPINILTINQLIPINNFCSDTVSCCSGEQIGLVNIQCTPILS#CCCCCSSCCCBHHHHHTTSCTTEEEEEECCHHHHTTCCSSCCCSSCCTTTEEECCHHHHHHCTTSBGGGSCCSSEEEEECCCTTCCSCCEEESCC", "chain_id": "", "gene_names": "MPG1, MGCH7_ch7g1089, MGG_10315", "r_value_free": "", "pdb_id": "2N4O", "reference": "Sci Rep. 2016 May 4;6:25288.", "keyword": "Hydrophobin-like protein MPG1", "protein_name": "Hydrophobin-like protein MPG1", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: SAIPAPGEGPSVSMAQQKCGAEKVVSCCNSKELKNSKSGAEIPIDVLSGECKNIPINILTINQLIPINNFCSDTVSCCSGEQIGLVNIQCTPILS", "entry": "S-0147", "length": "95", "uniprot_ac": "P52751", "author": "Pham, C.L., Rey, A., Lo, V., Soules, M., Ren, Q., Meisl, G., Knowles, T.P., Kwan, A.H., Sunde, M.", "ligand_smiles": "", "ligand_mw": "", "alternative_name": "", "ligand_name": "", "pdb_classification": "STRUCTURAL PROTEIN", "global_stoichiometry": "Monomer - A ", "inchi_key": "", "ligand_id": ""}