{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hsu MF"],"funding":["NIGMS NIH HHS"],"pagination":["105553"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10840475"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(1)"],"pubmed_abstract":["Proteins can spontaneously tie a variety of intricate topological knots through twisting and threading of the polypeptide chains. Recently developed artificial intelligence algorithms have predicted several new classes of topological knotted proteins, but the predictions remain to be authenticated experimentally. Here, we showed by X-ray crystallography and solution-state NMR spectroscopy that Q9PR55, an 89-residue protein from Ureaplasma urealyticum, possesses a novel 7<sub>1</sub> knotted topology that is accurately predicted by AlphaFold 2, except for the flexible N terminus. Q9PR55 is monomeric in solution, making it the smallest and most complex knotted protein known to date. In addition to its exceptional chemical stability against urea-induced unfolding, Q9PR55 is remarkably robust "],"journal":["The Journal of biological chemistry"],"pubmed_title":["Structure, dynamics, and stability of the smallest and most complex 7<sub>1</sub> protein knot."],"pmcid":["PMC10840475"],"funding_grant_id":["P41 GM111135"],"pubmed_authors":["Chen YR","Hsu SD","Lai CH","Hsu MF","Ko TP","Huang JS","Sriramoju MK","Huang KF"],"additional_accession":[]},"is_claimable":false,"name":"Structure, dynamics, and stability of the smallest and most complex 7<sub>1</sub> protein knot.","description":"Proteins can spontaneously tie a variety of intricate topological knots through twisting and threading of the polypeptide chains. Recently developed artificial intelligence algorithms have predicted several new classes of topological knotted proteins, but the predictions remain to be authenticated experimentally. Here, we showed by X-ray crystallography and solution-state NMR spectroscopy that Q9PR55, an 89-residue protein from Ureaplasma urealyticum, possesses a novel 7<sub>1</sub> knotted topology that is accurately predicted by AlphaFold 2, except for the flexible N terminus. Q9PR55 is monomeric in solution, making it the smallest and most complex knotted protein known to date. In addition to its exceptional chemical stability against urea-induced unfolding, Q9PR55 is remarkably robust ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jan","modification":"2026-05-29T10:07:14.015Z","creation":"2024-11-08T09:50:09.332Z"},"accession":"S-EPMC10840475","cross_references":{"pubmed":["38072060"],"doi":["10.1016/j.jbc.2023.105553"]}}