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• W2534401341 abstract "The recently determined crystal structure of the bacterial Na+-citrate symporter CitS provides unexpected structural and mechanistic insights. The protein has a fold that has not been seen in other proteins, but the oligomeric state, domain organization and proposed transport mechanism strongly resemble those of the sodium-dicarboxylate symporter vcINDY, and the putative exporters YdaH and MtrF, thus hinting at convergence in structure and function. CitS and the related proteins are predicted to translocate their substrates by an elevator-like mechanism, in which a compact transport domain slides up and down through the membrane while the dimerization domain is stably anchored. Here we review the large body of available biochemical data on CitS in the light of the new crystal structure. We show that the biochemical data are fully consistent with the proposed elevator mechanism, but also demonstrate that the current structural data cannot explain how strict coupling of citrate and Na+ transport is achieved. We propose a testable model for the coupling mechanism." @default.
• W2534401341 created "2016-10-28" @default.
• W2534401341 creator A5000910779 @default.
• W2534401341 creator A5075802016 @default.
• W2534401341 date "2017-08-01" @default.
• W2534401341 modified "2023-10-14" @default.
• W2534401341 title "Structure and elevator mechanism of the Na + -citrate transporter CitS" @default.
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• W2534401341 doi "https://doi.org/10.1016/j.sbi.2016.10.004" @default.
• W2534401341 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27776291" @default.
• W2534401341 hasPublicationYear "2017" @default.
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