Description
Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our high-resolution NMR results for a transmembrane protein, outer envelope protein of molar mass 16 kDa (OEP16), an

Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our high-resolution NMR results for a transmembrane protein, outer envelope protein of molar mass 16 kDa (OEP16), an amino acid transporter from the outer membrane of chloroplasts. Three-dimensional, high-resolution NMR experiments on the [superscript 13]C, [superscript 15]N, [superscript 2]H-triply-labeled protein were used to assign protein backbone resonances and to obtain secondary structure information. The results yield over 95% assignment of N, H[subscript N], CO, C[subscript α], and C[subscript β] chemical shifts, which is essential for obtaining a high resolution structure from NMR data. Chemical shift analysis from the assignment data reveals experimental evidence for the first time on the location of the secondary structure elements on a per residue basis. In addition T[subscript 1Z] and T[subscript 2] relaxation experiments were performed in order to better understand the protein dynamics. Arginine titration experiments yield an insight into the amino acid residues responsible for protein transporter function. The results provide the necessary basis for high-resolution structural determination of this important plant membrane protein.
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Title
  • High-Resolution NMR Reveals Secondary Structure and Folding of Amino Acid Transporter from Outer Chloroplast Membrane
Date Created
2013-10-29
Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1371/journal.pone.0078116
    • Identifier Type
      International standard serial number
      Identifier Value
      1045-3830
    • Identifier Type
      International standard serial number
      Identifier Value
      1939-1560
    Note
    • The article is published at http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0078116

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    Zook, J. D., Molugu, T. R., Jacobsen, N. E., Lin, G., Soll, J., Cherry, B. R., . . . Fromme, P. (2013). High-Resolution NMR Reveals Secondary Structure and Folding of Amino Acid Transporter from Outer Chloroplast Membrane. PLoS ONE, 8(10). doi:10.1371/journal.pone.0078116

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