4lep: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4lep]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis_MR-1 Shewanella oneidensis MR-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LEP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AFS:N-[(1R)-1-PHOSPHONOETHYL]-L-ALANINAMIDE'>AFS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AFS:N-[(1R)-1-PHOSPHONOETHYL]-L-ALANINAMIDE'>AFS</scene>, <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=4lep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lep OCA], [https://pdbe.org/4lep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lep RCSB], [https://www.ebi.ac.uk/pdbsum/4lep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lep ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/Q8EHE6_SHEON Q8EHE6_SHEON]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Short-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)-a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to target cells. Here, we present a structure of an oligomeric POT transporter from Shewanella oneidensis (PepTSo2), which was crystallized in the inward open conformation in complex with the peptidomimetic alafosfalin. All ligand-binding residues are highly conserved and the structural insights presented here are therefore likely to also apply to human POTs.
-Structural insights into substrate recognition in proton-dependent oligopeptide transporters.,Guettou F, Quistgaard EM, Tresaugues L, Moberg P, Jegerschold C, Zhu L, Jong AJ, Nordlund P, Low C EMBO Rep. 2013 Jul 19. doi: 10.1038/embor.2013.107. PMID:23867627<ref>PMID:23867627</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4lep" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Symporter 3D structures|Symporter 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>