{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kalli AC"],"funding":["Wellcome Trust","CIHR"],"pagination":["e1004123"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4346270"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(3)"],"pubmed_abstract":["The Escherichia coli UraA H+-uracil symporter is a member of the nucleobase/ascorbate transporter (NAT) family of proteins, and is responsible for the proton-driven uptake of uracil. Multiscale molecular dynamics simulations of the UraA symporter in phospholipid bilayers consisting of: 1) 1-palmitoyl 2-oleoyl-phosphatidylcholine (POPC); 2) 1-palmitoyl 2-oleoyl-phosphatidylethanolamine (POPE); and 3) a mixture of 75% POPE, 20% 1-palmitoyl 2-oleoyl-phosphatidylglycerol (POPG); and 5% 1-palmitoyl 2-oleoyl-diphosphatidylglycerol/cardiolipin (CL) to mimic the lipid composition of the bacterial inner membrane, were performed using the MARTINI coarse-grained force field to self-assemble lipids around the crystal structure of this membrane transport protein, followed by atomistic simulations. The "],"journal":["PLoS computational biology"],"pubmed_title":["Molecular dynamics simulations of the bacterial UraA H+-uracil symporter in lipid bilayers reveal a closed state and a selective interaction with cardiolipin."],"pmcid":["PMC4346270"],"funding_grant_id":["MOP102493","092970"],"pubmed_authors":["Kalli AC","Sansom MS","Reithmeier RA"],"additional_accession":[]},"is_claimable":false,"name":"Molecular dynamics simulations of the bacterial UraA H+-uracil symporter in lipid bilayers reveal a closed state and a selective interaction with cardiolipin.","description":"The Escherichia coli UraA H+-uracil symporter is a member of the nucleobase/ascorbate transporter (NAT) family of proteins, and is responsible for the proton-driven uptake of uracil. Multiscale molecular dynamics simulations of the UraA symporter in phospholipid bilayers consisting of: 1) 1-palmitoyl 2-oleoyl-phosphatidylcholine (POPC); 2) 1-palmitoyl 2-oleoyl-phosphatidylethanolamine (POPE); and 3) a mixture of 75% POPE, 20% 1-palmitoyl 2-oleoyl-phosphatidylglycerol (POPG); and 5% 1-palmitoyl 2-oleoyl-diphosphatidylglycerol/cardiolipin (CL) to mimic the lipid composition of the bacterial inner membrane, were performed using the MARTINI coarse-grained force field to self-assemble lipids around the crystal structure of this membrane transport protein, followed by atomistic simulations. The ","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Mar","modification":"2026-05-03T07:46:53.053Z","creation":"2019-03-26T22:41:29Z"},"accession":"S-EPMC4346270","cross_references":{"pubmed":["25729859"],"doi":["10.1371/journal.pcbi.1004123"]}}