SemiSWEET half glucose transporter of 93 aas and 3 TMSs with an N-terminal amphipathic α-helix. The protein occurs as a tight homodimer with the translocation channel between the two monomers. The 3-d structure is known at 2.4 Å resolution revealing the outward open conformation (Xu et al. 2014). The occluded state of the Vibrio sp. N418 SemiSWEET (9.A.58.3.1) has been solved at 1.7 Å resolution (Xu et al. 2014). The presence of these two states argues in favor of a carrier (rocker switch) mechanism rather than a channel-type mechanism (Xu et al. 2014).
|Protein Name:||Uncharacterized protein|
|Species:||Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)  |
|Number of TMSs:||3|
1: MENLIGYVAA FLTTVSFLPQ VLRVVMTKQT RDISRNMYIM FFLGVVLWFV YGILRSDLPI
61: ILANVVTLFF VTIILYYKLT EGNQT