期刊
BIOPHYSICAL JOURNAL
卷 96, 期 1, 页码 217-225出版社
CELL PRESS
DOI: 10.1016/j.bpj.2008.09.030
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资金
- Deutsche Forschungsgemeinschaft [Exc 114-1, Je246/3-2, Ju333/3-2, Ju333/4-2]
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 angstrom 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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