Advertisement

Biomolecular NMR Assignments

, Volume 3, Issue 1, pp 21–23 | Cite as

NMR assignments of the periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter

  • Tomas Jacso
  • Mathias Grote
  • Peter Schmieder
  • Erwin Schneider
  • Bernd Reif
Article

Abstract

We have assigned the 1H, 15N, 13C backbone resonances of the second periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter of Escherichia coli/Salmonella which is important for the recognition of the maltose binding protein MalE.

Keywords

ABC transporter Maltose transport Membrane protein 

Abbreviatons

ABC

ATP binding cassette

MalF-P2

Second periplasmic loop of MalF

MalF, MalG

Transmembrane subunits of the maltose transporter

MalE

Maltose binding protein

MalK

Intracellular nucleotide binding subunit

NBD

Nucleotide binding domain

Notes

Acknowledgments

This work was supported by the Leibniz-Gemeinschaft and the DFG (grants Re1435, Schn274/9–3, SFB 449, SFB 740)

References

  1. Boos W, Lucht JM (1996) Periplasmic binding protein-dependant ABC transporters. In: Neidhardt FC, Curtiss R, Ingraham JL, Lin ECC, Low KB, Magasanik B (eds) Ecoli and salmonella typhimurium: cellular and molecular biology. American Society for Microbiology Press, Washington, DC, pp 1175–1209Google Scholar
  2. Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289–302. doi: 10.1023/A:1008392405740 CrossRefGoogle Scholar
  3. Daus ML, Landmesser H, Schlosser A, Müller P, Herrmann A, Schneider E (2006) ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter. J Biol Chem 281:3856–3865. doi: 10.1074/jbc.M511953200 CrossRefGoogle Scholar
  4. Froshauer S, Green GN, Boyd D, McGovern K, Beckwith J (1988) Genetic analysis of the membrane insertion and topology of malf, a cytoplasmic membrane protein of Escherichia coli. J Mol Biol 200:501–511. doi: 10.1016/0022-2836(88)90539-6 CrossRefGoogle Scholar
  5. Higgins CF (1992) ABC TRANSPORTERS—from microorganisms to man. Annu Rev Cell Biol 8:67–113. doi: 10.1146/annurev.cb.08.110192.000435 CrossRefGoogle Scholar
  6. Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450:515–522. doi: 10.1038/nature06264 CrossRefADSGoogle Scholar
  7. Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog NMR Spect 34:93–158. doi: 10.1016/S0079-6565(98)00025-9 CrossRefGoogle Scholar
  8. Shilton BH, Shuman HA, Mowbray SL (1996) Crystal structures and solution conformations of a dominantnegative mutant of Ecoli maltose-binding protein. J Mol Biol 264:364–376. doi: 10.1006/jmbi.1996.0646 CrossRefGoogle Scholar
  9. Vranken WF, Boucher W, Stevens TJ, Pajon RFA, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59:687–696. doi: 10.1002/prot.20449 CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  • Tomas Jacso
    • 1
  • Mathias Grote
    • 2
  • Peter Schmieder
    • 1
  • Erwin Schneider
    • 2
  • Bernd Reif
    • 1
    • 3
  1. 1.Leibniz-Institut für Molekulare Pharmakologie (FMP)BerlinGermany
  2. 2.Institut für Biologie, AG BakterienphysiologieHumboldt-Universität zu BerlinBerlinGermany
  3. 3.Charité UniversitätsmedizinBerlinGermany

Personalised recommendations