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4qiq
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4qiq is ON HOLD Authors: Wisedchaisri, G., Park, M., Iadanza, M.G., Zheng, H., Gonen, T. Description: CRYSTAL STRUCTURE OF A PROTEIN) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of D-xylose-proton symporter== | |
| + | <StructureSection load='4qiq' size='340' side='right'caption='[[4qiq]], [[Resolution|resolution]] 3.51Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qiq]] 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=4QIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QIQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.51Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4qiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qiq OCA], [https://pdbe.org/4qiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qiq RCSB], [https://www.ebi.ac.uk/pdbsum/4qiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qiq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The major facilitator superfamily (MFS) is the largest collection of structurally related membrane proteins that transport a wide array of substrates. The proton-coupled sugar transporter XylE is the first member of the MFS that has been structurally characterized in multiple transporting conformations, including both the outward and inward-facing states. Here we report the crystal structure of XylE in a new inward-facing open conformation, allowing us to visualize the rocker-switch movement of the N-domain against the C-domain during the transport cycle. Using molecular dynamics simulation, and functional transport assays, we describe the movement of XylE that facilitates sugar translocation across a lipid membrane and identify the likely candidate proton-coupling residues as the conserved Asp27 and Arg133. This study addresses the structural basis for proton-coupled substrate transport and release mechanism for the sugar porter family of proteins. | ||
| - | + | Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE.,Wisedchaisri G, Park MS, Iadanza MG, Zheng H, Gonen T Nat Commun. 2014 Aug 4;5:4521. doi: 10.1038/ncomms5521. PMID:25088546<ref>PMID:25088546</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4qiq" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Symporter 3D structures|Symporter 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gonen T]] | ||
| + | [[Category: Iadanza MG]] | ||
| + | [[Category: Park M]] | ||
| + | [[Category: Wisedchaisri G]] | ||
| + | [[Category: Zheng H]] | ||
Current revision
Crystal structure of D-xylose-proton symporter
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