2018
DOI: 10.1038/s41598-018-20558-z
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A multidrug ABC transporter with a taste for GTP

Abstract: During the evolution of cellular bioenergetics, many protein families have been fashioned to match the availability and replenishment in energy supply. Molecular motors and primary transporters essentially need ATP to function while proteins involved in cell signaling or translation consume GTP. ATP-Binding Cassette (ABC) transporters are one of the largest families of membrane proteins gathering several medically relevant members that are typically powered by ATP hydrolysis. Here, a Streptococcus pneumoniae A… Show more

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Cited by 31 publications
(33 citation statements)
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References 64 publications
(81 reference statements)
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“…Previous studies showed that GTP-dependent Dox efflux by DrrAB-containing IOVs also occurs with higher efficiency as compared to with ATP [12], suggesting that at least in vitro GTP may be the preferred energy source for this transporter. A similar phenomenon was also observed in other ABC proteins, including PatA/PatB, OleB, and CvaB [4750], however its physiological relevance is currently unknown. Two significantly different nucleotide binding affinities observed in this study suggest that the two sites in DrrA behave in an asymmetric fashion, and this asymmetry is further accentuated by mutations in the A-loop and Walker A motifs.…”
Section: Discussionsupporting
confidence: 67%
“…Previous studies showed that GTP-dependent Dox efflux by DrrAB-containing IOVs also occurs with higher efficiency as compared to with ATP [12], suggesting that at least in vitro GTP may be the preferred energy source for this transporter. A similar phenomenon was also observed in other ABC proteins, including PatA/PatB, OleB, and CvaB [4750], however its physiological relevance is currently unknown. Two significantly different nucleotide binding affinities observed in this study suggest that the two sites in DrrA behave in an asymmetric fashion, and this asymmetry is further accentuated by mutations in the A-loop and Walker A motifs.…”
Section: Discussionsupporting
confidence: 67%
“…Although λDE3 is normally dormant in the host chromosome, the expression of toxic proteins may results in the induction of the SOS cascade that directly or indirectly damage the E. coli chromosome leading to cell lysis. The expression of PatA/PatB was induced overnight at 25 °C by IPTG addition at high OD 600 nm (~1.7), as published before 13,14 . In addition, the BL21(DE3) strain was either induced by IPTG or by using an auto-induction media.…”
Section: Resultsmentioning
confidence: 99%
“…The first one is the heterodimeric PatA/PatB transporter from Streptococcus pneumoniae . Although its biochemical characterization is at early stages 13,14 , its implication in clinical resistance to antibiotics was clearly demonstrated by the group of Piddock 1517 . The second one is the homodimeric BmrA transporter from Bacillus subtilis 18 .…”
Section: Introductionmentioning
confidence: 99%
“…Using multiple protein-protein network and structure comparison, I-TASSER deducted Lip.JG3 to have the most similar function with template protein of Fe 3+ ions import ATP-binding protein FbpC since it showed a high score in C-Score (0.89). Although this template protein (PDB Hit: 3fvqA) acts as a transport protein, it is classified into hydrolase superfamily since ABC Transporter Protein is able to hydrolyze ATP to power up its act [28][29]. On the other hand, Lip.JG3's 3D model has the highest similarity with ABC-ATPase (PDB Hit: 1OXT) based on TM-align structural alignment program to match the model of all structures in the PDB library with TM score up to 0.939 [30].…”
Section: Prediction Of Lipase Jg3 3d Structurementioning
confidence: 99%