Backbone Structure of Transmembrane Domain IX of the Na+/Proline Transporter PutP of Escherichia coli

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2009
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Hilger, Daniel
Polyhach, Yevhen
Jung, Heinrich
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https://doi.org/10.1016/j.bpj.2008.09.030
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Biophysical Journal. Cell Press. 2009, 96(1), pp. 217-225. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2008.09.030
Zusammenfassung

The backbone structure is determined by site-directed spin labeling, double electron electron resonance measurements of distances, and modeling in terms of a helix-loop-helix construct for a transmembrane domain that is supposed to line the translocation pathway in the 54.3 kDa Na+/proline symporter PutP of Escherichia coli. The conformational distribution of the spin labels is accounted for by a rotamer library. An ensemble of backbone models with a root mean-square deviation of less than 2 Å is obtained. These models exhibit a pronounced kink near residue T341, which is involved in substrate binding. The kink may be associated with a hinge that allows the protein to open and close an inwardly oriented cavity.

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ISO 690HILGER, Daniel, Yevhen POLYHACH, Heinrich JUNG, Gunnar JESCHKE, 2009. Backbone Structure of Transmembrane Domain IX of the Na+/Proline Transporter PutP of Escherichia coli. In: Biophysical Journal. Cell Press. 2009, 96(1), pp. 217-225. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2008.09.030
BibTex
@article{Hilger2009-01Backb-58510,
  year={2009},
  doi={10.1016/j.bpj.2008.09.030},
  title={Backbone Structure of Transmembrane Domain IX of the Na<sup>+</sup>/Proline Transporter PutP of Escherichia coli},
  number={1},
  volume={96},
  issn={0006-3495},
  journal={Biophysical Journal},
  pages={217--225},
  author={Hilger, Daniel and Polyhach, Yevhen and Jung, Heinrich and Jeschke, Gunnar}
}
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