SemiSWEET half putative sugar transporter of 97 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 1.7 Å resolution revealing the occluded
conformation (Xu et al. 2014). The outward open state of the Leptospira biflexa SemiSWEET (2.a.123.2.6) has been solved at 2.4 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:||Putative uncharacterized protein|
|Species:||Vibrio sp. N418  |
|Number of TMSs:||3|
1: MALIERIGKA LEPLMLVMGL ISPLATMPQL YKLYVSHSEH ALGLSLTTWL LYSFIALLWT
61: IYGIYHKNPT IWVGNCLGFL MYVAMVVGII AHTGGTY