<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zhang H</submitter><funding>NIGMS NIH HHS</funding><pagination>38324-36</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2992266</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>285(49)</volume><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complex.</pubmed_title><pmcid>PMC2992266</pmcid><funding_grant_id>R01 GM51981-09</funding_grant_id><funding_grant_id>R01 GM051981</funding_grant_id><pubmed_authors>Pradhan P</pubmed_authors><pubmed_authors>Zhang H</pubmed_authors><pubmed_authors>Kaur P</pubmed_authors></additional><is_claimable>false</is_claimable><name>The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complex.</name><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</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Dec</publication><modification>2026-04-30T23:27:47.586Z</modification><creation>2019-03-27T00:36:55Z</creation></dates><accession>S-EPMC2992266</accession><cross_references><pubmed>20876527</pubmed><doi>10.1074/jbc.m110.131540</doi><doi>10.1074/jbc.M110.131540</doi></cross_references></HashMap>