{"reference": "Sci Rep. 2016 Apr 21;6:24656.", "alternative_name": "", "entry": "S-0148", "gene_names": "Rpdx1_1250", "remarks": "Solution Structure of R. palustris CsgH", "secondary_structure": "MVQCEVEAAVSGGHVTLQGVITAVRDGAGSYKLAVDKAGAAGTSRIKQAGAFTAIAEQRVTVGNVVLDYSSANRYAARLDVSFGSVTIQCNLDPETVKLEHHHHHH#CBCCCCEEEEETTEEEEEEEEEESSSEEEEEEEEEEEEETTEEEEEEEEEEEEECBTEEEEEEEEEEECCTTSEEEEEEEEEETTEEEEEECCGGGCSSCCCCCCC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Non-amyloid", "pmid": "27098162", "ligand_smiles": "", "keyword": "Putative uncharacterized protein CsgH", "peptide_protein_sequence": "chain-ID A: MVQCEVEAAVSGGHVTLQGVITAVRDGAGSYKLAVDKAGAAGTSRIKQAGAFTAIAEQRVTVGNVVLDYSSANRYAARLDVSFGSVTIQCNLDPETVKLEHHHHHH", "uniprot_ac": "E6VF87", "protein_name": "Uncharacterized protein", "r_value_free": "", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "2N59", "inchi_key": "", "ec_number": "", "pdb_classification": "UNKNOWN FUNCTION", "type": "Protein", "author": "Taylor, J.D., Hawthorne, W.J., Lo, J., Dear, A., Jain, N., Meisl, G., Andreasen, M., Fletcher, C., Koch, M., Darvill, N., Scull, N., Escalera-Maurer, A., Sefer, L., Wenman, R., Lambert, S., Jean, J., Xu, Y., Turner, B., Kazarian, S.G., Chapman, M.R., Bube", "species": "Rhodopseudomonas palustris", "ligand_id": "", "method": "SOLUTION NMR", "ligand_name": "", "global_stoichiometry": "Monomer - A ", "resolution": "", "ligand_formula": "", "length": "106", "ligstr": "", "description": "<amyloid inhibitor> An Escherichia protein, CsgC potently inhibits amyloid formation of curli amyloid proteins. Here, they unlock its mechanism of action, and show that CsgC strongly inhibits primary nucleation via electrostatically-guided molecular encounters, which expands the conformational distribution of disordered curli subunits. This delays the formation of higher order intermediates and maintains amyloidogenic subunits in a secretion-competent form. "}