PDBsum entry 4zw9

Transport protein

PDB id: 4zw9

Contents

Protein chain

470 a.a.

Ligands

OLC ×3

GLC

BGC

Waters ×101

PDB id:

4zw9

Name:

Transport protein

Title:

Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom

Structure:

Solute carrier family 2, facilitated glucose transporter member 3. Chain: a. Synonym: glucose transporter type 3,brain,glut-3. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: slc2a3, glut3. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.

Resolution:

1.50Å R-factor: 0.184 R-free: 0.199

Authors:

D.Deng,P.C.Sun,C.Y.Yan,N.Yan

Key ref:

D.Deng et al. (2015). Molecular basis of ligand recognition and transport by glucose transporters. Nature, 526, 391-396. PubMed id: 26176916 DOI: 10.1038/nature14655

Date:

19-May-15 Release date: 22-Jul-15

Protein chain

P11169  (GTR3_HUMAN) -  Solute carrier family 2, facilitated glucose transporter member 3 from Homo sapiens

Seq: 496 a.a.

Struc: 470 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1038/nature14655

Nature 526:391-396 (2015)

PubMed id: 26176916

Molecular basis of ligand recognition and transport by glucose transporters.

D.Deng, P.Sun, C.Yan, M.Ke, X.Jiang, L.Xiong, W.Ren, K.Hirata, M.Yamamoto, S.Fan, N.Yan.

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.