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Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli
Y. Huang, M. J. Lemieux, J. Song, M. Auer, D.-N. Wang
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Supporting Online Material
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This supplement contains:
Materials and Methods
Figs. S1 to S4
References
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To view these movies, download a QuickTime viewer.
- Movie S1
Structure of GlpT viewed from within the membrane. The helixes are colored in the
same scheme as for Fig. 2.
- Movie S2
Proposed rocker-switch type conformational changes accompany substrate
translocation by GlpT. The crystal structure determined in this work represents the Ci
conformation of the protein. The Co-S conformation was generated by fitting the GlpT model into the 6.5 Å map of the substrate-bound form of OxlT (S11). By separately rotating the two halves of the GlpT model in opposite directions along an axis at the interface and parallel to the membrane, we found that a ~6° rotation by each domain can generate a structure that fits the OxlT map reasonably well. The Co conformation was produced by a ~10° rotation by each domain that is sufficient to close the pore on the cytosolic side of the molecule and to open a pore on the periplasmic side. Finally, the Ci-S conformation was generated by a ~4° rotation.
