5m8a: Difference between revisions

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'''Unreleased structure'''


The entry 5m8a is ON HOLD  until Paper Publication
==Crystal structure of Eremococcus coleocola manganese transporter mutant E129A==
<StructureSection load='5m8a' size='340' side='right' caption='[[5m8a]], [[Resolution|resolution]] 3.90&Aring;' 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.


Authors: Manatschal, C., Ehrnstorfer, I.A., Arnold, F.M., Laederach, J., Dutzler, R.
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: Crystal structure of Eremococcus coleocola manganese transporter mutant E129A
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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: Arnold, F.M]]
[[Category: Ehrnstorfer, I A]]
[[Category: Ehrnstorfer, I.A]]
[[Category: Laederach, J]]
[[Category: Manatschal, C]]
[[Category: Manatschal, C]]
[[Category: Laederach, J]]
[[Category: Transport protein]]
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