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Tellurite-resistance/dicarboxylate transporter

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C4dic_mal_tran
Identifiers
SymbolC4dic_mal_tran
PfamPF03595
InterProIPR004695
TCDB2.A.16
OPM superfamily213
OPM protein3m73
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Two members of the Tellurite-Resistance/Dicarboxylate Transporter (TDT) family have been functionally characterised. One is the TehA protein of Escherichia coli which has been implicated in resistance to tellurite; the other is the Mae1 protein of Schizosaccharomyces pombe which functions in the uptake of malate and other dicarboxylates by a proton symport mechanism. These proteins have 10 putative transmembrane helices.[1][2]

References

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  1. ^ Chen YH, Hu L, Punta M, Bruni R, Hillerich B, Kloss B, Rost B, Love J, Siegelbaum SA, Hendrickson WA (October 2010). "Homologue structure of the SLAC1 anion channel for closing stomata in leaves". Nature. 467 (7319): 1074–80. Bibcode:2010Natur.467.1074C. doi:10.1038/nature09487. PMC 3548404. PMID 20981093.
  2. ^ Vahisalu T, Kollist H, Wang YF, Nishimura N, Chan WY, Valerio G, Lamminmäki A, Brosché M, Moldau H, Desikan R, Schroeder JI, Kangasjärvi J (March 2008). "SLAC1 is required for plant guard cell S-type anion channel function in stomatal signalling". Nature. 452 (7186): 487–91. Bibcode:2008Natur.452..487V. doi:10.1038/nature06608. PMC 2858982. PMID 18305484.
This article incorporates text from the public domain Pfam and InterPro: IPR004695