{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cao Z"],"funding":["Dezhou University Doctoral Fund Project","Youth Innovation Team Lead-education Project of Shandong Educational Committee","National Natural Science Foundation of China (NSFC)"],"pagination":["542"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10537873"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(9)"],"pubmed_abstract":["Previous experimental investigations have established the indispensability of the C-terminal Lys-Arg residues in the toxic activity of the AapA1 toxin protein. AapA1 is classified as a type I toxin-antitoxin (TA) bacterial toxin, and the precise impact of the C-terminal Lys-Arg residues on its structure and mechanism of action remains elusive. To address this knowledge gap, the present study employed molecular dynamics (MD) and enhanced sampling Well-tempered Two-dimensional Metadynamics (2D-MetaD) simulations to examine the behavior of the C-terminal Lys-Arg residues of truncated AapA1 toxin (AapA1-28) within the inner membrane of <i>Escherichia coli</i>. Specifically, the study focused on the elucidation of possible conformation states of AapA1-28 protein in POPE/POPG (3:1) bilayers and "],"journal":["Toxins"],"pubmed_title":["Effects of C-Terminal Lys-Arg Residue of AapA1 Protein on Toxicity and Structural Mechanism."],"pmcid":["PMC10537873"],"funding_grant_id":["2019xjrc206","32171249","31670727"],"pubmed_authors":["Zhao L","Liu L","Cao Z","Yan T"],"additional_accession":[]},"is_claimable":false,"name":"Effects of C-Terminal Lys-Arg Residue of AapA1 Protein on Toxicity and Structural Mechanism.","description":"Previous experimental investigations have established the indispensability of the C-terminal Lys-Arg residues in the toxic activity of the AapA1 toxin protein. AapA1 is classified as a type I toxin-antitoxin (TA) bacterial toxin, and the precise impact of the C-terminal Lys-Arg residues on its structure and mechanism of action remains elusive. To address this knowledge gap, the present study employed molecular dynamics (MD) and enhanced sampling Well-tempered Two-dimensional Metadynamics (2D-MetaD) simulations to examine the behavior of the C-terminal Lys-Arg residues of truncated AapA1 toxin (AapA1-28) within the inner membrane of <i>Escherichia coli</i>. Specifically, the study focused on the elucidation of possible conformation states of AapA1-28 protein in POPE/POPG (3:1) bilayers and ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Sep","modification":"2026-04-07T15:55:10.498Z","creation":"2025-02-19T01:20:05.013Z"},"accession":"S-EPMC10537873","cross_references":{"pubmed":["37755968"],"doi":["10.3390/toxins15090542"]}}