View source for 4qiq


==Crystal structure of D-xylose-proton symporter==
<StructureSection load='4qiq' size='340' side='right'caption='[[4qiq]], [[Resolution|resolution]] 3.51&Aring;' 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]] 3.51&#8491;</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&reg;/PubMed&reg;, 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]]