4ZWB
Crystal structure of maltose-bound human GLUT3 in the outward-occluded conformation at 2.4 angstrom
Summary for 4ZWB
| Entry DOI | 10.2210/pdb4zwb/pdb |
| Related | 4ZW9 4ZWC |
| Related PRD ID | PRD_900001 |
| Descriptor | Solute carrier family 2, facilitated glucose transporter member 3, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | transporter, transport protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 56816.79 |
| Authors | |
| Primary citation | Deng, D.,Sun, P.C.,Yan, C.Y.,Ke, M.,Jiang, X.,Xiong, L.,Ren, W.,Hirata, K.,Yamamoto, M.,Fan, S.,Yan, N. Molecular basis of ligand recognition and transport by glucose transporters Nature, 526:391-396, 2015 Cited by PubMed Abstract: 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 Å resolution in an outward-occluded conformation. The high-resolution structure allows discrimination of both α- and β-anomers of D-glucose. Two additional structures of GLUT3 bound to the exofacial inhibitor maltose were obtained at 2.6 Å in the outward-open and 2.4 Å 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. PubMed: 26176916DOI: 10.1038/nature14655 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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