6tl2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Eremococcus coleocola manganese transporter in complex with an aromatic bis-isothiourea substituted compound== | |
| + | <StructureSection load='6tl2' size='340' side='right'caption='[[6tl2]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6tl2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TL2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NJZ:[3-bromanyl-5-(carbamimidoylsulfanylmethyl)phenyl]methyl+carbamimidothioate'>NJZ</scene></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=6tl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tl2 OCA], [http://pdbe.org/6tl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tl2 RCSB], [http://www.ebi.ac.uk/pdbsum/6tl2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tl2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/E4KPW4_9LACT E4KPW4_9LACT]] H(+)-stimulated, divalent metal cation uptake system.[HAMAP-Rule:MF_00221] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In humans, the divalent metal ion transporter-1 (DMT1) mediates the transport of ferrous iron across the apical membrane of enterocytes. Hence, its inhibition could be beneficial for the treatment of iron overload disorders. Here we characterize the interaction of aromatic bis-isothiourea-substituted compounds with human DMT1 and its prokaryotic homologue EcoDMT. Both transporters are inhibited by a common competitive mechanism with potencies in the low micromolar range. The crystal structure of EcoDMT in complex with a brominated derivative defines the binding of the inhibitor to an extracellular pocket of the transporter in direct contact with residues of the metal ion coordination site, thereby interfering with substrate loading and locking the transporter in its outward-facing state. Mutagenesis and structure-activity relationships further support the observed interaction mode and reveal species-dependent differences between pro- and eukaryotic transporters. Together, our data provide the first detailed mechanistic insight into the pharmacology of SLC11/NRAMP transporters. | ||
| - | + | Mechanistic basis of the inhibition of SLC11/NRAMP-mediated metal ion transport by bis-isothiourea substituted compounds.,Manatschal C, Pujol-Gimenez J, Poirier M, Reymond JL, Hediger MA, Dutzler R Elife. 2019 Dec 5;8. pii: 51913. doi: 10.7554/eLife.51913. PMID:31804182<ref>PMID:31804182</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6tl2" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Dutzler, R]] | [[Category: Dutzler, R]] | ||
| + | [[Category: Manatschal, C]] | ||
| + | [[Category: Inhibitor complex]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 07:56, 18 December 2019
Crystal structure of Eremococcus coleocola manganese transporter in complex with an aromatic bis-isothiourea substituted compound
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