5m8a
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Eremococcus coleocola manganese transporter mutant E129A== | |
| + | <StructureSection load='5m8a' size='340' side='right' caption='[[5m8a]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m8a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M8A FirstGlance]. <br> | ||
| + | </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=5m8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m8a OCA], [http://pdbe.org/5m8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m8a RCSB], [http://www.ebi.ac.uk/pdbsum/5m8a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m8a 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 == | ||
| + | Secondary active transporters of the SLC11/NRAMP family catalyse the uptake of iron and manganese into cells. These proteins are highly conserved across all kingdoms of life and thus likely share a common transport mechanism. Here we describe the structural and functional properties of the prokaryotic SLC11 transporter EcoDMT. Its crystal structure reveals a previously unknown outward-facing state of the protein family. In proteoliposomes EcoDMT mediates proton-coupled uptake of manganese at low micromolar concentrations. Mutants of residues in the transition-metal ion-binding site severely affect transport, whereas a mutation of a conserved histidine located near this site results in metal ion transport that appears uncoupled to proton transport. Combined with previous results, our study defines the conformational changes underlying transition-metal ion transport in the SLC11 family and it provides molecular insight to its coupling to protons. | ||
| - | + | Structural and mechanistic basis of proton-coupled metal ion transport in the SLC11/NRAMP family.,Ehrnstorfer IA, Manatschal C, Arnold FM, Laederach J, Dutzler R Nat Commun. 2017 Jan 6;8:14033. doi: 10.1038/ncomms14033. PMID:28059071<ref>PMID:28059071</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5m8a" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arnold, F M]] | ||
[[Category: Dutzler, R]] | [[Category: Dutzler, R]] | ||
| - | + | [[Category: Ehrnstorfer, I A]] | |
| - | [[Category: Ehrnstorfer, I | + | |
| - | + | ||
[[Category: Laederach, J]] | [[Category: Laederach, J]] | ||
| + | [[Category: Manatschal, C]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 07:35, 18 January 2017
Crystal structure of Eremococcus coleocola manganese transporter mutant E129A
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