ABCB7 p.Glu523Gln
| Predicted by SNAP2: | A: N (53%), C: N (66%), D: N (97%), F: D (66%), G: D (66%), H: N (57%), I: D (63%), K: D (75%), L: D (66%), M: D (59%), N: N (61%), P: D (66%), Q: N (57%), R: D (66%), S: D (59%), T: N (53%), V: D (59%), W: D (71%), Y: D (63%), |
| Predicted by PROVEAN: | A: D, C: D, D: N, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: N, R: D, S: D, T: D, V: D, W: D, Y: D, |
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[hide] Structural basis for heavy metal detoxification by... Science. 2014 Mar 7;343(6175):1133-6. doi: 10.1126/science.1246489. Lee JY, Yang JG, Zhitnitsky D, Lewinson O, Rees DC
Structural basis for heavy metal detoxification by an Atm1-type ABC exporter.
Science. 2014 Mar 7;343(6175):1133-6. doi: 10.1126/science.1246489., [PMID:24604198]
Abstract [show]
Although substantial progress has been achieved in the structural analysis of exporters from the superfamily of adenosine triphosphate (ATP)-binding cassette (ABC) transporters, much less is known about how they selectively recognize substrates and how substrate binding is coupled to ATP hydrolysis. We have addressed these questions through crystallographic analysis of the Atm1/ABCB7/HMT1/ABCB6 ortholog from Novosphingobium aromaticivorans DSM 12444, NaAtm1, at 2.4 angstrom resolution. Consistent with a physiological role in cellular detoxification processes, functional studies showed that glutathione derivatives can serve as substrates for NaAtm1 and that its overexpression in Escherichia coli confers protection against silver and mercury toxicity. The glutathione binding site highlights the articulated design of ABC exporters, with ligands and nucleotides spanning structurally conserved elements to create adaptable interfaces accommodating conformational rearrangements during the transport cycle.
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No. Sentence Comment
48 (A) Amount of GSSG transported per milligram of protein accumulated inside vesicles prepared from E. coli membranes overexpressing wild-type NaAtm1 or the E523Q (Glu523 Gln) Walker B motif ATPase-defective mutant.
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ABCB7 p.Glu523Gln 24604198:48:155
status: NEW