New breakthrough in structural biology!

After the nutrients are digested, they are absorbed in the intestines

In the 1960s, this question was initially answered, and the concept of co-transport with secondary active transporters was proposed

For more than half a century, the physiological function and transport mechanism of SGLT1 have been extensively studied

However, people have a very limited understanding of the structure of the SGLT family for a long time

It is extremely challenging for researchers to reveal the cryo-EM structure of SGLT1

In this regard, the research team adopted a series of innovative strategies: As the SGLT1 protein is small, the authors used high-affinity nanobodies to significantly increase the characteristics of the protein extra-membrane region, which makes it easier for them to classify and structure protein particles.

These work significantly improved the observability of the SGLT1 protein.

▲The cryo-EM structure of SGLT1 (picture source: reference [1])

The structure of cryo-electron microscopy shows that the SGLT1 protein is similar to the prokaryotic leucine transporter (LeuT), consisting of a supporting domain and a transport domain

From the protein structure, the researchers also discovered the mechanism by which SGLT1 recognizes sugar molecules

▲Schematic diagram of the transfer mechanism between SGLT1 and SGLT2 (picture source: reference [2])

This study also found that SGLT1 has a structural basis for water channel activity

Note: The original text has been deleted

Reference materials:

[1] Lei Han et al.

[2] David Drew, Structures show how salt gets a sweet ride.