View source for 5kte


==Crystal structure of Deinococcus radiodurans MntH, an Nramp-family transition metal transporter==
<StructureSection load='5kte' size='340' side='right'caption='[[5kte]], [[Resolution|resolution]] 3.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kte]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KTE 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]] 3.941&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OS:OSMIUM+ION'>OS</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=5kte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kte OCA], [https://pdbe.org/5kte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kte RCSB], [https://www.ebi.ac.uk/pdbsum/5kte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kte ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MNTH_DEIRA MNTH_DEIRA] H(+)-stimulated, divalent metal cation uptake system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The widely conserved natural resistance-associated macrophage protein (Nramp) family of divalent metal transporters enables manganese import in bacteria and dietary iron uptake in mammals. We determined the crystal structure of the Deinococcus radiodurans Nramp homolog (DraNramp) in an inward-facing apo state, including the complete transmembrane (TM) segment 1a (absent from a previous Nramp structure). Mapping our cysteine accessibility scanning results onto this structure, we identified the metal-permeation pathway in the alternate outward-open conformation. We investigated the functional impact of two natural anemia-causing glycine-to-arginine mutations that impaired transition metal transport in both human Nramp2 and DraNramp. The TM4 G153R mutation perturbs the closing of the outward metal-permeation pathway and alters the selectivity of the conserved metal-binding site. In contrast, the TM1a G45R mutation prevents conformational change by sterically blocking the essential movement of that helix, thus locking the transporter in an inward-facing state.

Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.,Bozzi AT, Bane LB, Weihofen WA, Singharoy A, Guillen ER, Ploegh HL, Schulten K, Gaudet R Structure. 2016 Dec 6;24(12):2102-2114. doi: 10.1016/j.str.2016.09.017. Epub 2016, Nov 10. PMID:27839948<ref>PMID:27839948</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kte" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Deinococcus radiodurans R1]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Bane LB]]
[[Category: Gaudet R]]
[[Category: Singharoy A]]
[[Category: Weihofen WA]]