4x5m: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4x5m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UMEA_3162-1 Escherichia coli UMEA 3162-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X5M FirstGlance]. <br>
<table><tr><td colspan='2'>[[4x5m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UMEA_3162-1 Escherichia coli UMEA 3162-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X5M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4x5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5m OCA], [https://pdbe.org/4x5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x5m RCSB], [https://www.ebi.ac.uk/pdbsum/4x5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x5m 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=4x5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5m OCA], [https://pdbe.org/4x5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x5m RCSB], [https://www.ebi.ac.uk/pdbsum/4x5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x5m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/SWEET_ECOU3 SWEET_ECOU3] The homodimer mediates transmembrane sugar transport down a concentration gradient. Transport is probably effected by rocking-type movements, where a cargo-binding cavity opens first on one and then on the other side of the membrane.<ref>PMID:25598322</ref>  
[https://www.uniprot.org/uniprot/SWEET_ECOU3 SWEET_ECOU3] The homodimer mediates transmembrane sugar transport down a concentration gradient. Transport is probably effected by rocking-type movements, where a cargo-binding cavity opens first on one and then on the other side of the membrane.<ref>PMID:25598322</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SWEET family proteins mediate sugar transport across biological membranes and play crucial roles in plants and animals. The SWEETs and their bacterial homologues, the SemiSWEETs, are related to the PQ-loop family, which is characterized by highly conserved proline and glutamine residues (PQ-loop motif). Although the structures of the bacterial SemiSWEETs were recently reported, the conformational transition and the significance of the conserved motif in the transport cycle have remained elusive. Here we report crystal structures of SemiSWEET from Escherichia coli, in the both inward-open and outward-open states. A structural comparison revealed that SemiSWEET undergoes an intramolecular conformational change in each protomer. The conserved PQ-loop motif serves as a molecular hinge that enables the 'binder clip-like' motion of SemiSWEET. The present work provides the framework for understanding the overall transport cycles of SWEET and PQ-loop family proteins.
Structural basis for the facilitative diffusion mechanism by SemiSWEET transporter.,Lee Y, Nishizawa T, Yamashita K, Ishitani R, Nureki O Nat Commun. 2015 Jan 19;6:6112. doi: 10.1038/ncomms7112. PMID:25598322<ref>PMID:25598322</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4x5m" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 09:02, 20 March 2024

Crystal structure of SemiSWEET in the inward-open conformation

4x5m, resolution 2.00Å

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