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4gc0
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4gc0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GC0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4gc0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GC0 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6BG:6-BROMO-6-DEOXY-BETA-D-GLUCOPYRANOSE'>6BG</scene>, <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</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]] 2.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6BG:6-BROMO-6-DEOXY-BETA-D-GLUCOPYRANOSE'>6BG</scene>, <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene></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=4gc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gc0 OCA], [https://pdbe.org/4gc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gc0 RCSB], [https://www.ebi.ac.uk/pdbsum/4gc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gc0 ProSAT]</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=4gc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gc0 OCA], [https://pdbe.org/4gc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gc0 RCSB], [https://www.ebi.ac.uk/pdbsum/4gc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gc0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/XYLE_ECOLI XYLE_ECOLI] Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system). | [https://www.uniprot.org/uniprot/XYLE_ECOLI XYLE_ECOLI] Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system). | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Glucose transporters are essential for metabolism of glucose in cells of diverse organisms from microbes to humans, exemplified by the disease-related human proteins GLUT1, 2, 3 and 4. Despite rigorous efforts, the structural information for GLUT1-4 or their homologues remains largely unknown. Here we report three related crystal structures of XylE, an Escherichia coli homologue of GLUT1-4, in complex with d-xylose, d-glucose and 6-bromo-6-deoxy-D-glucose, at resolutions of 2.8, 2.9 and 2.6 A, respectively. The structure consists of a typical major facilitator superfamily fold of 12 transmembrane segments and a unique intracellular four-helix domain. XylE was captured in an outward-facing, partly occluded conformation. Most of the important amino acids responsible for recognition of D-xylose or d-glucose are invariant in GLUT1-4, suggesting functional and mechanistic conservations. Structure-based modelling of GLUT1-4 allows mapping and interpretation of disease-related mutations. The structural and biochemical information reported here constitutes an important framework for mechanistic understanding of glucose transporters and sugar porters in general. | ||
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| - | Crystal structure of a bacterial homologue of glucose transporters GLUT1-4.,Sun L, Zeng X, Yan C, Sun X, Gong X, Rao Y, Yan N Nature. 2012 Oct 18;490(7420):361-6. doi: 10.1038/nature11524. PMID:23075985<ref>PMID:23075985</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4gc0" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Symporter 3D structures|Symporter 3D structures]] | *[[Symporter 3D structures|Symporter 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
The structure of the MFS (major facilitator superfamily) proton:xylose symporter XylE bound to 6-bromo-6-deoxy-D-glucose
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