4zw9

Crystal structure of human GLUT3 bound to D-glucose in the outward-occluded conformation at 1.5 angstrom

spinqualitylabelsall models 4zw9, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zw9 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 1.502Å Ligands: BGC, GLC, OLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease GTR3_HUMAN Huntington disease. Function GTR3_HUMAN Facilitative glucose transporter. Probably a neuronal glucose transporter. Publication Abstract from PubMed The major facilitator superfamily glucose transporters, exemplified by human GLUT1-4, have been central to the study of solute transport. Using lipidic cubic phase crystallization and microfocus X-ray diffraction, we determined the structure of human GLUT3 in complex with d-glucose at 1.5 A resolution in an outward-occluded conformation. The high-resolution structure allows discrimination of both alpha- and beta-anomers of d-glucose. Two additional structures of GLUT3 bound to the exofacial inhibitor maltose were obtained at 2.6 A in the outward-open and 2.4 A in the outward-occluded states. In all three structures, the ligands are predominantly coordinated by polar residues from the carboxy terminal domain. Conformational transition from outward-open to outward-occluded entails a prominent local rearrangement of the extracellular part of transmembrane segment TM7. Comparison of the outward-facing GLUT3 structures with the inward-open GLUT1 provides insights into the alternating access cycle for GLUTs, whereby the C-terminal domain provides the primary substrate-binding site and the amino-terminal domain undergoes rigid-body rotation with respect to the C-terminal domain. Our studies provide an important framework for the mechanistic and kinetic understanding of GLUTs and shed light on structure-guided ligand design. Molecular basis of ligand recognition and transport by glucose transporters.,Deng D, Sun P, Yan C, Ke M, Jiang X, Xiong L, Ren W, Hirata K, Yamamoto M, Fan S, Yan N Nature. 2015 Jul 15. doi: 10.1038/nature14655. PMID:26176916 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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