Difference between revisions of "ECF transporter"

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(Important reviews and publications)
(The substrate-specific S components of the ECF transporters)
 
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* [[TrpP]]: uptake of tryptophan
 
* [[TrpP]]: uptake of tryptophan
 
* [[YuiG]]: unknown specificity, may also transport biotin
 
* [[YuiG]]: unknown specificity, may also transport biotin
 +
* [[YpdP]]: queuosine precursor uptake
 +
 +
== The class I ECF transporter for thiamine ==
 +
* [[ThiU]]: binding protein
 +
* [[ThiV]]: substrate-specific S component
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* [[ThiW]]: ATP-binding protein (corresponds to A1 + A2)
 +
* [[ThiX]]: membrane-spanning T protein
  
 
== Important reviews and publications ==
 
== Important reviews and publications ==
 
<pubmed>23584589 , 21135102, 20497229, 18931129 22574898 24362466 27273632</pubmed>
 
<pubmed>23584589 , 21135102, 20497229, 18931129 22574898 24362466 27273632</pubmed>

Latest revision as of 17:42, 26 March 2024

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transport proteins


ECF transporters are required for the uptake of micronutrients such as cofactors (vitamins), metal ions, or amino acids. The transporters are composed of three general components (membrane spanning T protein und two ATP-hydrolyzing A proteins) and substrate-specific S proteins. In B. subtilis, there are four known substrates for ECF transporters, riboflavin, thiamine, biotin, and tryptophan.

The general components of the ECF transporters

  • ybxA ATP-binding A1 protein (EcfA1)
  • ybaE ATP-binding A2 protein (EcfA2)
  • ybaF membrane-spanning T protein (EcfT)

The substrate-specific S components of the ECF transporters

  • RibU: uptake of riboflavin
  • ThiT: uptake of thiamine
  • YhfU: uptake of biotin
  • TrpP: uptake of tryptophan
  • YuiG: unknown specificity, may also transport biotin
  • YpdP: queuosine precursor uptake

The class I ECF transporter for thiamine

  • ThiU: binding protein
  • ThiV: substrate-specific S component
  • ThiW: ATP-binding protein (corresponds to A1 + A2)
  • ThiX: membrane-spanning T protein

Important reviews and publications

Kaspar P Locher
Mechanistic diversity in ATP-binding cassette (ABC) transporters.
Nat Struct Mol Biol: 2016, 23(6);487-93
[PubMed:27273632] [WorldCat.org] [DOI] (I p)

Dirk J Slotboom
Structural and mechanistic insights into prokaryotic energy-coupling factor transporters.
Nat Rev Microbiol: 2014, 12(2);79-87
[PubMed:24362466] [WorldCat.org] [DOI] (I p)

Ke Xu, Minhua Zhang, Qin Zhao, Fang Yu, Hui Guo, Chengyuan Wang, Fangyuan He, Jianping Ding, Peng Zhang
Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis.
Nature: 2013, 497(7448);268-71
[PubMed:23584589] [WorldCat.org] [DOI] (I p)

Guus B Erkens, Maria Majsnerowska, Josy ter Beek, Dirk Jan Slotboom
Energy coupling factor-type ABC transporters for vitamin uptake in prokaryotes.
Biochemistry: 2012, 51(22);4390-6
[PubMed:22574898] [WorldCat.org] [DOI] (I p)

Josy ter Beek, Ria H Duurkens, Guus B Erkens, Dirk Jan Slotboom
Quaternary structure and functional unit of energy coupling factor (ECF)-type transporters.
J Biol Chem: 2011, 286(7);5471-5
[PubMed:21135102] [WorldCat.org] [DOI] (I p)

Thomas Eitinger, Dmitry A Rodionov, Mathias Grote, Erwin Schneider
Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
FEMS Microbiol Rev: 2011, 35(1);3-67
[PubMed:20497229] [WorldCat.org] [DOI] (I p)

Dmitry A Rodionov, Peter Hebbeln, Aymerick Eudes, Josy ter Beek, Irina A Rodionova, Guus B Erkens, Dirk J Slotboom, Mikhail S Gelfand, Andrei L Osterman, Andrew D Hanson, Thomas Eitinger
A novel class of modular transporters for vitamins in prokaryotes.
J Bacteriol: 2009, 191(1);42-51
[PubMed:18931129] [WorldCat.org] [DOI] (I p)