5m87: Difference between revisions

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'''Unreleased structure'''


The entry 5m87 is ON HOLD
==Crystal structure of Eremococcus coleocola manganese transporter==
<StructureSection load='5m87' size='340' side='right'caption='[[5m87]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5m87]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eremococcus_coleocola_ACS-139-V-Col8 Eremococcus coleocola ACS-139-V-Col8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M87 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]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</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=5m87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m87 OCA], [https://pdbe.org/5m87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m87 RCSB], [https://www.ebi.ac.uk/pdbsum/5m87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m87 ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5m87" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Eremococcus coleocola ACS-139-V-Col8]]
[[Category: Large Structures]]
[[Category: Arnold FM]]
[[Category: Dutzler R]]
[[Category: Ehrnstorfer IA]]
[[Category: Laederach J]]
[[Category: Manatschal C]]
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