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Paulsen, P. A.

Publications and source records attributed to Paulsen, P. A..

2 recordsLinked to original sources

Molecular mechanism of high affinity sugar transport in plants unveiled by structures of glucose/H+ symporter STP10

Sugars are essential sources of energy and carbon, and also function as key signaling molecules in plants. Sugar Transport Proteins (STP) are proton-coupled symporters, solely responsible for uptake of glucose from the apoplastic compartment into cells in all plant tissues. They are integral to organ development in symplastically isolated tissues such as seeds, pollen and fruit. Additionally, STPs play a significant role in plant responses to both environmental stressors such as dehydration, and prevalent fungal infections like rust and mildew. Here, we present two high-resolution crystal structures of the outward-occluded and inward-open conformations of Arabidopsis thaliana STP10 with glucose and protons bound. The two structures describe key states in the STP transport cycle. Together with in vivo biochemical analysis and Molecular Dynamics simulations they pinpoint structural elements that explain how STPs exhibit high affinity for sugar binding on the extracellular side and how it is considerably lowered on the intracellular side to facilitate substrate release. These structural elements, conserved in all STPs across plant species, clarify the basis of proton-to-glucose coupling, essential for symport. The results advance our understanding of a key molecular mechanism behind plant organ development, and sets the stage for novel bioengineering strategies in crops that could target seeds, fruits and plant resistance to fungal infections.

plant biology↗

Structural comparative analysis of GLUT1 and GLUT3 reveal role of SP motif in transport regulation

The human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. GLUT1 and GLUT3 share a fully conserved substrate-binding site with identical substrate coordination, but differ significantly in transport affinity in line with their physiological function. Here we present a 2.4 [A] crystal structure of GLUT1 in an inward open conformation and compare it with GLUT3 using both structural and functional data. Our work shows that interactions between a cytosolic "Sugar Porter motif" and a conserved "A motif" stabilize the outward conformational state and increases substrate apparent affinity. Furthermore, we identify a previously undescribed Cl- ion site in GLUT1 and an endofacial lipid/glucose binding site which modulate GLUT kinetics. The results provide a possible explanation for the difference between GLUT1 and GLUT3 glucose affinity, imply a general model for the kinetic regulation in GLUTs and suggest a physiological function for the defining SP sequence motif in the Sugar Porter family. Summary BlurbNew structure of GLUT1 compared to GLUT3 explain different substrate affinities. The result provide a functional rationale for key structural motifs that define the universal Sugar Porter family.

biochemistry↗