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

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

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HILGER, 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. 96(1), pp. 217-225. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2008.09.030

@article{Hilger2009-01Backb-58510, title={Backbone Structure of Transmembrane Domain IX of the Na+/Proline Transporter PutP of Escherichia coli}, year={2009}, doi={10.1016/j.bpj.2008.09.030}, 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} }

Polyhach, Yevhen 2009-01 eng Jeschke, Gunnar Hilger, Daniel 2022-09-06T13:30:18Z 2022-09-06T13:30:18Z Jung, Heinrich Jeschke, Gunnar 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<sup>+</sup>/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. Backbone Structure of Transmembrane Domain IX of the Na<sup>+</sup>/Proline Transporter PutP of Escherichia coli Jung, Heinrich Polyhach, Yevhen Hilger, Daniel

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