6tha

Crystal structure of human sugar transporter GLUT1 (SLC2A1) in the inward conformation

spinqualitylabelsall models 6tha, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6tha is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: BNG, CL, P33 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease GTR1_HUMAN Hereditary cryohydrocytosis with reduced stomatin;Paroxysmal exertion-induced dyskinesia;Encephalopathy due to GLUT1 deficiency;Paroxysmal dystonic choreathetosis with episodic ataxia and spasticity;Childhood absence epilepsy;Epilepsy with myoclonic-astatic seizures. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function GTR1_HUMAN Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses. Publication Abstract from PubMed 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 "SP 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 SP family. Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family.,Custodio TF, Paulsen PA, Frain KM, Pedersen BP Life Sci Alliance. 2021 Feb 3;4(4). pii: 4/4/e202000858. doi:, 10.26508/lsa.202000858. Print 2021 Apr. PMID:33536238 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

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