ABCB1 p.Lys380Ala
| Predicted by SNAP2: | A: N (57%), C: D (53%), D: N (78%), E: N (87%), F: D (63%), G: N (57%), H: N (53%), I: N (66%), L: N (61%), M: N (66%), N: N (82%), P: N (78%), Q: N (72%), R: N (82%), S: N (72%), T: N (87%), V: N (61%), W: D (63%), Y: D (63%), |
| Predicted by PROVEAN: | A: N, C: D, D: N, E: N, F: D, G: D, H: N, I: D, L: D, M: N, N: N, P: N, Q: N, R: N, S: N, T: N, V: N, W: D, Y: D, |
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[hide] Characterization of YvcC (BmrA), a multidrug ABC t... Biochemistry. 2004 Jun 15;43(23):7491-502. Steinfels E, Orelle C, Fantino JR, Dalmas O, Rigaud JL, Denizot F, Di Pietro A, Jault JM
Characterization of YvcC (BmrA), a multidrug ABC transporter constitutively expressed in Bacillus subtilis.
Biochemistry. 2004 Jun 15;43(23):7491-502., 2004-06-15 [PMID:15182191]
Abstract [show]
The involvement of transporters in multidrug resistance of bacteria is an increasingly challenging problem, and most of the pumps identified so far use the protonmotive gradient as the energy source. A new member of the ATP-binding cassette (ABC) family, known in Bacillus subtilis as YvcC and homologous to each half of mammalian P-glycoprotein and to LmrA of Lactococcus lactis, has been studied here. The yvcC gene was constitutively expressed in B. subtilis throughout its growth, and a knockout mutant showed a lower rate of ethidium efflux than the wild-type strain. Overexpression of yvcC in Escherichia coli allowed the preparation of highly enriched inverted-membrane vesicles that exhibited high transport activities of three fluorescent drugs, namely, Hoechst 33342, doxorubicin, and 7-aminoactinomycin D. After solubilization with n-dodecyl beta-D-maltoside, the hexahistidine-tagged YvcC was purified by a one-step affinity chromatography, and its ability to bind many P-glycoprotein effectors was evidenced by fluorescence spectroscopy experiments. Collectively, these results showed that YvcC is a multidrug ABC transporter functionally active in wild-type B. subtilis, and YvcC was therefore renamed BmrA for Bacillus multidrug resistance ATP. Besides, reconstitution of YvcC into liposomes led to the highest, vanadate-sensitive, ATPase activity reported so far for an ABC transporter. Interestingly, such a high ATP hydrolysis proceeds with a positive cooperativity mechanism, a property only found so far with ABC importers.
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122 A similar result was also obtained with the K380A mutant, which is totally devoid of ATPase activity (not shown).
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ABCB1 p.Lys380Ala 15182191:122:44
status: NEW173 Furthermore, no ATPase activity was detected when purified E504A, E504Q [corresponding to the catalytic base of ABC transporters (47)], or K380A YvcC mutant was used, ruling out the possibility that the ATPase activity seen with the wild-type YvcC might be due to a contaminant.
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ABCB1 p.Lys380Ala 15182191:173:139
status: NEW