6d91

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'''Unreleased structure'''
 
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The entry 6d91 is ON HOLD until Paper Publication
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==Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter in the outward-open, apo conformation==
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<StructureSection load='6d91' size='340' side='right'caption='[[6d91]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6d91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D91 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.356&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d91 OCA], [https://pdbe.org/6d91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d91 RCSB], [https://www.ebi.ac.uk/pdbsum/6d91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d91 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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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Authors: Bozzi, A.T., Zimanyi, C.Z., Nicoludis, J.M., Gaudet, R.
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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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Description: Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter in the outward-open, apo conformation
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Gaudet, R]]
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<div class="pdbe-citations 6d91" style="background-color:#fffaf0;"></div>
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[[Category: Nicoludis, J.M]]
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== References ==
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[[Category: Zimanyi, C.Z]]
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<references/>
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[[Category: Bozzi, A.T]]
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__TOC__
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</StructureSection>
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[[Category: Deinococcus radiodurans R1]]
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[[Category: Large Structures]]
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[[Category: Bozzi AT]]
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[[Category: Gaudet R]]
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[[Category: Nicoludis JM]]
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[[Category: Zimanyi CM]]

Current revision

Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter in the outward-open, apo conformation

PDB ID 6d91

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