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==Crystal structure of maltose-bound human GLUT3 in the outward-open conformation at 2.6 angstrom==
==Crystal structure of maltose-bound human GLUT3 in the outward-open conformation at 2.6 angstrom==
<StructureSection load='4zwc' size='340' side='right' caption='[[4zwc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='4zwc' size='340' side='right'caption='[[4zwc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4zwc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZWC FirstGlance]. <br>
<table><tr><td colspan='2'>[[4zwc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZWC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zw9|4zw9]], [[4zwb|4zwb]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zwc RCSB], [http://www.ebi.ac.uk/pdbsum/4zwc PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zwc OCA], [https://pdbe.org/4zwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zwc RCSB], [https://www.ebi.ac.uk/pdbsum/4zwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zwc ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/GTR3_HUMAN GTR3_HUMAN]] Huntington disease.
[https://www.uniprot.org/uniprot/GTR3_HUMAN GTR3_HUMAN] Huntington disease.  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GTR3_HUMAN GTR3_HUMAN]] Facilitative glucose transporter. Probably a neuronal glucose transporter.  
[https://www.uniprot.org/uniprot/GTR3_HUMAN GTR3_HUMAN] Facilitative glucose transporter. Probably a neuronal glucose transporter.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:26176916</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zwc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Deng, D]]
[[Category: Homo sapiens]]
[[Category: Sun, P C]]
[[Category: Large Structures]]
[[Category: Yan, C Y]]
[[Category: Deng D]]
[[Category: Yan, N]]
[[Category: Sun PC]]
[[Category: Transport protein]]
[[Category: Yan CY]]
[[Category: Transporter]]
[[Category: Yan N]]
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