{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gonti S"],"funding":["NCRR NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["643-647"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8991541"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["60(9)"],"pubmed_abstract":["The anthrax toxin protective antigen (PA), the membrane binding and pore-forming component of the anthrax toxin, was studied using <sup>19</sup>F NMR. We site-specifically labeled PA with <i>p</i>-fluorophenylalanine (pF-Phe) at Phe427, a critically important residue that comprises the ϕ-clamp that is required for translocation of edema factor (EF) and lethal factor (LF) into the host cell cytosol. We utilized <sup>19</sup>F NMR to follow low-pH-induced structural changes in the prepore, alone and bound to the N-terminal PA binding domain of LF, LF<sub>N</sub>. Our studies indicate that pF-Phe427 is dynamic in the prepore state and then becomes more dynamic in the transition to the pore. An increase in dynamic behavior at the ϕ-clamp may provide the necessary room for movement needed in tr"],"journal":["Biochemistry"],"pubmed_title":["Site-Specific Labeling and <sup>19</sup>F NMR Provide Direct Evidence for Dynamic Behavior of the Anthrax Toxin Pore ϕ-Clamp Structure."],"pmcid":["PMC8991541"],"funding_grant_id":["P20 GM103418","S10 RR029220","S10 RR023438","S10 RR025062","S10 RR008438","P41 GM103399","S10 RR002781","P41 RR002301","P20 RR017708"],"pubmed_authors":["Westler WM","Gonti S","Miyagi M","Bann JG"],"additional_accession":[]},"is_claimable":false,"name":"Site-Specific Labeling and <sup>19</sup>F NMR Provide Direct Evidence for Dynamic Behavior of the Anthrax Toxin Pore ϕ-Clamp Structure.","description":"The anthrax toxin protective antigen (PA), the membrane binding and pore-forming component of the anthrax toxin, was studied using <sup>19</sup>F NMR. We site-specifically labeled PA with <i>p</i>-fluorophenylalanine (pF-Phe) at Phe427, a critically important residue that comprises the ϕ-clamp that is required for translocation of edema factor (EF) and lethal factor (LF) into the host cell cytosol. We utilized <sup>19</sup>F NMR to follow low-pH-induced structural changes in the prepore, alone and bound to the N-terminal PA binding domain of LF, LF<sub>N</sub>. Our studies indicate that pF-Phe427 is dynamic in the prepore state and then becomes more dynamic in the transition to the pore. An increase in dynamic behavior at the ϕ-clamp may provide the necessary room for movement needed in tr","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2026-05-31T06:03:18.064Z","creation":"2025-02-19T01:55:25.235Z"},"accession":"S-EPMC8991541","cross_references":{"pubmed":["33428379"],"doi":["10.1021/acs.biochem.0c00833"]}}