Research About The Structure Of Vitamin B1 Transporter THI10

Vitamins are crucial components in the diet ofanimals and many other living organisms. One of theseessential nutrients, thiamin, is known to be involved in several cell functions, including energy metabolism and the degradationof sugars and carbon skeletons. Other roles that areconnected to this vitamin are neuronal communication, immune system activation, signaling and maintenanceprocesses in cells and tissues, and cell-membrane dynamics.Because of the key functions of thiamin, uptake and transportthrough the body are crucial. Its uptake route is relativelycomplex, encompassing a variety of protein families, includingthe solute carrier anion transporters, the alkaline phosphatasetransport system, and the human extraneuronal monoamine transporter family, some of which are multispecific proteins. Thereare two known structures of protein (subunits) involved in thiamin uptake in prokaryotes. Binding of thiamin to these proteins isstrongly guided by electrostatic interactions. The lack of structural information about thiamin binding proteins for higherorganisms remains a bottleneck for understanding the uptake process of thiamin in atomic detail. THI10, from saccharomyces cerevisiae, is a VB1 transporter protein. Structural features of THI10 may help understand the mechanism of VB1 uptake and transport. Also this could indicate solution to clinical VB1 deficience.