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5cth

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Revision as of 17:09, 18 August 2017

The 3.7 A resolution structure of a eukaryotic SWEET transporter

Structural highlights

5cth is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	5ctg
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SWT2B_ORYSJ] Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.[UniProtKB:Q8L9J7]

Publication Abstract from PubMed

Eukaryotes rely on efficient distribution of energy and carbon skeletons between organs in the form of sugars. Glucose in animals and sucrose in plants serve as the dominant distribution forms. Cellular sugar uptake and release require vesicular and/or plasma membrane transport proteins. Humans and plants use proteins from three superfamilies for sugar translocation: the major facilitator superfamily (MFS), the sodium solute symporter family (SSF; only in the animal kingdom), and SWEETs. SWEETs carry mono- and disaccharides across vacuolar or plasma membranes. Plant SWEETs play key roles in sugar translocation between compartments, cells, and organs, notably in nectar secretion, phloem loading for long distance translocation, pollen nutrition, and seed filling. Plant SWEETs cause pathogen susceptibility possibly by sugar leakage from infected cells. The vacuolar Arabidopsis thaliana AtSWEET2 sequesters sugars in root vacuoles; loss-of-function mutants show increased susceptibility to Pythium infection. Here we show that its orthologue, the vacuolar glucose transporter OsSWEET2b from rice (Oryza sativa), consists of an asymmetrical pair of triple-helix bundles, connected by an inversion linker transmembrane helix (TM4) to create the translocation pathway. Structural and biochemical analyses show OsSWEET2b in an apparent inward (cytosolic) open state forming homomeric trimers. TM4 tightly interacts with the first triple-helix bundle within a protomer and mediates key contacts among protomers. Structure-guided mutagenesis of the close paralogue SWEET1 from Arabidopsis identified key residues in substrate translocation and protomer crosstalk. Insights into the structure-function relationship of SWEETs are valuable for understanding the transport mechanism of eukaryotic SWEETs and may be useful for engineering sugar flux.

Structure of a eukaryotic SWEET transporter in a homotrimeric complex.,Tao Y, Cheung LS, Li S, Eom JS, Chen LQ, Xu Y, Perry K, Frommer WB, Feng L Nature. 2015 Nov 12;527(7577):259-63. doi: 10.1038/nature15391. Epub 2015 Oct 19. PMID:26479032^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tao Y, Cheung LS, Li S, Eom JS, Chen LQ, Xu Y, Perry K, Frommer WB, Feng L. Structure of a eukaryotic SWEET transporter in a homotrimeric complex. Nature. 2015 Nov 12;527(7577):259-63. doi: 10.1038/nature15391. Epub 2015 Oct 19. PMID:26479032 doi:http://dx.doi.org/10.1038/nature15391

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5cth"

@@ Line 1: / Line 1: @@
 ==The 3.7 A resolution structure of a eukaryotic SWEET transporter==
 <StructureSection load='5cth' size='340' side='right' caption='[[5cth]], [[Resolution|resolution]] 3.69&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ctg|5ctg]]</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=5cth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cth OCA], [http://pdbe.org/5cth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cth RCSB], [http://www.ebi.ac.uk/pdbsum/5cth PDBsum]</span></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=5cth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cth OCA], [http://pdbe.org/5cth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cth RCSB], [http://www.ebi.ac.uk/pdbsum/5cth PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cth ProSAT]</span></td></tr>
 </table>
 == Function ==

5cth

From Proteopedia

Revision as of 17:09, 18 August 2017

The 3.7 A resolution structure of a eukaryotic SWEET transporter

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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