ABCB2 p.Ser105Cys
| Predicted by SNAP2: | A: N (66%), C: D (63%), D: D (63%), E: D (75%), F: D (75%), G: D (63%), H: D (71%), I: D (75%), K: D (75%), L: D (53%), M: D (59%), N: D (53%), P: D (80%), Q: D (71%), R: D (71%), T: N (93%), V: D (71%), W: D (85%), Y: D (75%), |
| Predicted by PROVEAN: | A: N, C: D, D: N, E: N, F: D, G: N, H: N, I: D, K: N, L: D, M: N, N: N, P: N, Q: N, R: N, T: N, V: N, W: D, Y: D, |
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[hide] Crystal structure of a heterodimeric ABC transport... Nat Struct Mol Biol. 2012 Mar 25;19(4):395-402. doi: 10.1038/nsmb.2267. Hohl M, Briand C, Grutter MG, Seeger MA
Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation.
Nat Struct Mol Biol. 2012 Mar 25;19(4):395-402. doi: 10.1038/nsmb.2267., [PMID:22447242]
Abstract [show]
ATP-binding cassette (ABC) transporters shuttle a wide variety of molecules across cell membranes by alternating between inward- and outward-facing conformations, harnessing the energy of ATP binding and hydrolysis at their nucleotide binding domains (NBDs). Here we present the 2.9-A crystal structure of the heterodimeric ABC transporter TM287-TM288 (TM287/288) from Thermotoga maritima in its inward-facing state. In contrast to previous studies, we found that the NBDs only partially separate, remaining in contact through an interface involving conserved motifs that connect the two ATP hydrolysis sites. We observed AMP-PNP binding to the degenerate catalytic site, which deviates from the consensus sequence in the same positions as the eukaryotic homologs CFTR and TAP1-TAP2 (TAP1/2). The TM287/288 structure provides unprecedented insights into the mechanism of heterodimeric ABC exporters and will enable future studies on this large transporter superfamily.
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No. Sentence Comment
430 A cysteine-less TM287/288 clone (see Supplementary Methods) served as template for the introduction of the -single mutants TM287(S105C) and TM288(T486C) and the corresponding double mutant.MutantTM287/288waspurifiedandincubatedwithcopperphenanthroline (1mM)andnucleotides(2.5mM)asindicatedinBufferAcontaining3mMMgCl2 at roomtemperaturefor20min.Thecross-linkedproteinwasseparatedbynonreducing SDS-PAGE and quantified by SYPRO ruby staining (Invitrogen).
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ABCB2 p.Ser105Cys 22447242:430:129
status: NEW