{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Van V"],"funding":["NIGMS NIH HHS","NIH HHS"],"pagination":["167816"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9992452"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["434(21)"],"pubmed_abstract":["Eukaryotic post-translational arginylation, mediated by the family of enzymes known as the arginyltransferases (ATE1s), is an important post-translational modification that can alter protein function and even dictate cellular protein half-life. Multiple major biological pathways are linked to the fidelity of this process, including neural and cardiovascular developments, cell division, and even the stress response. Despite this significance, the structural, mechanistic, and regulatory mechanisms that govern ATE1 function remain enigmatic. To that end, we have used X-ray crystallography to solve the crystal structure of ATE1 from the model organism Saccharomyces cerevisiae ATE1 (ScATE1) in the apo form. The three-dimensional structure of ScATE1 reveals a bilobed protein containing a GCN5-re"],"journal":["Journal of molecular biology"],"pubmed_title":["The Structure of Saccharomyces cerevisiae Arginyltransferase 1 (ATE1)."],"pmcid":["PMC9992452"],"funding_grant_id":["S10 OD018483","R35 GM133497","T34 GM136497","P30 GM124169"],"pubmed_authors":["Van V","Smith AT","Bui TS","Ejimogu NE"],"additional_accession":[]},"is_claimable":false,"name":"The Structure of Saccharomyces cerevisiae Arginyltransferase 1 (ATE1).","description":"Eukaryotic post-translational arginylation, mediated by the family of enzymes known as the arginyltransferases (ATE1s), is an important post-translational modification that can alter protein function and even dictate cellular protein half-life. Multiple major biological pathways are linked to the fidelity of this process, including neural and cardiovascular developments, cell division, and even the stress response. Despite this significance, the structural, mechanistic, and regulatory mechanisms that govern ATE1 function remain enigmatic. To that end, we have used X-ray crystallography to solve the crystal structure of ATE1 from the model organism Saccharomyces cerevisiae ATE1 (ScATE1) in the apo form. The three-dimensional structure of ScATE1 reveals a bilobed protein containing a GCN5-re","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-28T11:20:31.846Z","creation":"2025-02-19T03:05:25.062Z"},"accession":"S-EPMC9992452","cross_references":{"pubmed":["36087779"],"doi":["10.1016/j.jmb.2022.167816"]}}