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| - | | + | #REDIRECT [[8e6n]] This PDB entry is obsolete and replaced by 8e6n |
| - | ==Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter in the outward-open, manganese-bound conformation==
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| - | <StructureSection load='6bu5' size='340' side='right' caption='[[6bu5]], [[Resolution|resolution]] 2.40Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[6bu5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Deira Deira]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BU5 FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mntH, DR_1709 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243230 DEIRA])</td></tr>
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| - | <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=6bu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bu5 OCA], [http://pdbe.org/6bu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bu5 RCSB], [http://www.ebi.ac.uk/pdbsum/6bu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bu5 ProSAT]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/MNTH_DEIRA MNTH_DEIRA]] H(+)-stimulated, divalent metal cation uptake system.
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Nramp family transporters-expressed in organisms from bacteria to humans-enable uptake of essential divalent transition metals via an alternating-access mechanism that also involves proton transport. We present high-resolution structures of Deinococcus radiodurans (Dra)Nramp in multiple conformations to provide a thorough description of the Nramp transport cycle by identifying the key intramolecular rearrangements and changes to the metal coordination sphere. Strikingly, while metal transport requires cycling from outward- to inward-open states, efficient proton transport still occurs in outward-locked (but not inward-locked) DraNramp. We propose a model in which metal and proton enter the transporter via the same external pathway to the binding site, but follow separate routes to the cytoplasm, which could facilitate the co-transport of two cationic species. Our results illustrate the flexibility of the LeuT fold to support a broad range of substrate transport and conformational change mechanisms.
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| - | Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter.,Bozzi AT, Zimanyi CM, Nicoludis JM, Lee BK, Zhang CH, Gaudet R Elife. 2019 Feb 4;8. pii: 41124. doi: 10.7554/eLife.41124. PMID:30714568<ref>PMID:30714568</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 6bu5" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Deira]]
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| - | [[Category: Bozzi, A T]]
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| - | [[Category: Gaudet, R]]
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| - | [[Category: Nicoludis, J M]]
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| - | [[Category: Zimanyi, C M]]
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| - | [[Category: Divalent transition metal transporter]]
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| - | [[Category: Leut-fold]]
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| - | [[Category: Manganese importer]]
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| - | [[Category: Proton-coupled secondary transporter]]
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| - | [[Category: Transport protein]]
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