biostudies-literatureZhang HNational institutes of HealthMolecular Basis of Disease ProgramNIGMS NIH HHS148-53https://www.ebi.ac.uk/biostudies/studies/S-EPMC4363271biostudies-literatureUnknown459(1)A novel domain, GATE (Glycine-loop And Transducer Element), is identified in the ABC protein DrrA. This domain shows sequence and structural conservation among close homologs of DrrA as well as distantly-related ABC proteins. Among the highly conserved residues in this domain are three glycines, G215, G221 and G231, of which G215 was found to be critical for stable expression of the DrrAB complex. Other conserved residues, including E201, G221, K227 and G231, were found to be critical for the catalytic and transport functions of the DrrAB transporter. Structural analysis of both the previously published crystal structure of the DrrA homolog MalK and the modeled structure of DrrA showed that G215 makes close contacts with residues in and around the Walker A motif, suggesting that these inteBiochemical and biophysical research communicationsCharacterization of a novel domain 'GATE' in the ABC protein DrrA and its role in drug efflux by the DrrAB complex.PMC4363271R01 GM51981-09RO1 GM51981-09R01 GM051981Li WRahman SZhang HFu GKaur PfalseCharacterization of a novel domain 'GATE' in the ABC protein DrrA and its role in drug efflux by the DrrAB complex.A novel domain, GATE (Glycine-loop And Transducer Element), is identified in the ABC protein DrrA. This domain shows sequence and structural conservation among close homologs of DrrA as well as distantly-related ABC proteins. Among the highly conserved residues in this domain are three glycines, G215, G221 and G231, of which G215 was found to be critical for stable expression of the DrrAB complex. Other conserved residues, including E201, G221, K227 and G231, were found to be critical for the catalytic and transport functions of the DrrAB transporter. Structural analysis of both the previously published crystal structure of the DrrA homolog MalK and the modeled structure of DrrA showed that G215 makes close contacts with residues in and around the Walker A motif, suggesting that these inte2015-01-01T00:00:00Z2015 Mar2026-04-13T14:08:02.156Z2019-03-27T01:48:21ZS-EPMC43632712572166510.1016/j.bbrc.2015.02.086