{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang H"],"funding":["NIGMS NIH HHS"],"pagination":["38324-36"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2992266"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["285(49)"],"pubmed_abstract":["Two novel regulatory motifs, LDEVFL and C-terminal regulatory Glu (E)-rich motif (CREEM), are identified in the extreme C terminus of the ABC protein DrrA, which is involved in direct interaction with the N-terminal cytoplasmic tail of the membrane protein DrrB and in homodimerization of DrrA. Disulfide cross-linking analysis showed that the CREEM and the region immediately upstream of CREEM participate directly in forming an interaction interface with the N terminus of DrrB. A series of mutations created in the LDEVFL and CREEM motifs drastically affected overall function of the DrrAB transporter. Mutations in the LDEVFL motif also significantly impaired interaction between the C terminus of DrrA and the N terminus of DrrB as well as the ability of DrrA and DrrB to co-purify, therefore su"],"journal":["The Journal of biological chemistry"],"pubmed_title":["The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complex."],"pmcid":["PMC2992266"],"funding_grant_id":["R01 GM51981-09","R01 GM051981"],"pubmed_authors":["Pradhan P","Zhang H","Kaur P"],"additional_accession":[]},"is_claimable":false,"name":"The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complex.","description":"Two novel regulatory motifs, LDEVFL and C-terminal regulatory Glu (E)-rich motif (CREEM), are identified in the extreme C terminus of the ABC protein DrrA, which is involved in direct interaction with the N-terminal cytoplasmic tail of the membrane protein DrrB and in homodimerization of DrrA. Disulfide cross-linking analysis showed that the CREEM and the region immediately upstream of CREEM participate directly in forming an interaction interface with the N terminus of DrrB. A series of mutations created in the LDEVFL and CREEM motifs drastically affected overall function of the DrrAB transporter. Mutations in the LDEVFL motif also significantly impaired interaction between the C terminus of DrrA and the N terminus of DrrB as well as the ability of DrrA and DrrB to co-purify, therefore su","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Dec","modification":"2026-04-30T23:27:47.586Z","creation":"2019-03-27T00:36:55Z"},"accession":"S-EPMC2992266","cross_references":{"pubmed":["20876527"],"doi":["10.1074/jbc.m110.131540","10.1074/jbc.M110.131540"]}}