{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bagde SR"],"funding":["NIMHD NIH HHS","NIGMS NIH HHS"],"pagination":["723-729"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8689591"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["374(6568)"],"pubmed_abstract":["Type I modular polyketide synthases are homodimeric multidomain assembly line enzymes that synthesize a variety of polyketide natural products by performing polyketide chain extension and β-keto group modification reactions. We determined the 2.4-angstrom-resolution x-ray crystal structure and the 3.1-angstrom-resolution cryo–electron microscopy structure of the Lsd14 polyketide synthase, stalled at the transacylation and condensation steps, respectively. These structures revealed how the constituent domains are positioned relative to each other, how they rearrange depending on the step in the reaction cycle, and the specific interactions formed between the domains. Like the evolutionarily related mammalian fatty acid synthase, Lsd14 contains two reaction chambers, but only one chamber in "],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Modular polyketide synthase contains two reaction chambers that operate asynchronously."],"pmcid":["PMC8689591"],"funding_grant_id":["R35 GM136258","P41 GM103393","R01 GM138990","U54 MD007592"],"pubmed_authors":["Kim CY","Mathews II","Fromme JC","Bagde SR"],"additional_accession":[]},"is_claimable":false,"name":"Modular polyketide synthase contains two reaction chambers that operate asynchronously.","description":"Type I modular polyketide synthases are homodimeric multidomain assembly line enzymes that synthesize a variety of polyketide natural products by performing polyketide chain extension and β-keto group modification reactions. We determined the 2.4-angstrom-resolution x-ray crystal structure and the 3.1-angstrom-resolution cryo–electron microscopy structure of the Lsd14 polyketide synthase, stalled at the transacylation and condensation steps, respectively. These structures revealed how the constituent domains are positioned relative to each other, how they rearrange depending on the step in the reaction cycle, and the specific interactions formed between the domains. Like the evolutionarily related mammalian fatty acid synthase, Lsd14 contains two reaction chambers, but only one chamber in ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2026-05-30T15:08:14.834Z","creation":"2025-04-04T23:03:19.475Z"},"accession":"S-EPMC8689591","cross_references":{"pubmed":["34735234"],"doi":["10.1126/science.abi8532"]}}