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.
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Abbreviations
- 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
References
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) E. coli and salmonella typhimurium: cellular and molecular biology. American Society for Microbiology Press, Washington, DC, pp 1175–1209
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
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
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
Higgins CF (1992) ABC TRANSPORTERS—from microorganisms to man. Annu Rev Cell Biol 8:67–113. doi:10.1146/annurev.cb.08.110192.000435
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
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
Shilton BH, Shuman HA, Mowbray SL (1996) Crystal structures and solution conformations of a dominantnegative mutant of E. coli maltose-binding protein. J Mol Biol 264:364–376. doi:10.1006/jmbi.1996.0646
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
Acknowledgments
This work was supported by the Leibniz-Gemeinschaft and the DFG (grants Re1435, Schn274/9–3, SFB 449, SFB 740)
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Jacso, T., Grote, M., Schmieder, P. et al. NMR assignments of the periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter. Biomol NMR Assign 3, 21–23 (2009). https://doi.org/10.1007/s12104-008-9131-7
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DOI: https://doi.org/10.1007/s12104-008-9131-7