8e6n
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==X-ray structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter G223W mutant in an outward-open, manganese-bound state== | |
+ | <StructureSection load='8e6n' size='340' side='right'caption='[[8e6n]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[8e6n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6bu5 6bu5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8E6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E6N FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</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=8e6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e6n OCA], [https://pdbe.org/8e6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e6n RCSB], [https://www.ebi.ac.uk/pdbsum/8e6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e6n 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 == | ||
+ | Transporters of the Nramp (Natural resistance-associated macrophage protein) family import divalent transition metal ions into cells of most organisms. By supporting metal homeostasis, Nramps prevent diseases and disorders related to metal insufficiency or overload. Previous studies revealed that Nramps take on a LeuT fold and identified the metal-binding site. We present high-resolution structures of Deinococcus radiodurans (Dra)Nramp in three stable conformations of the transport cycle revealing that global conformational changes are supported by distinct coordination geometries of its physiological substrate, Mn(2+), across conformations, and by conserved networks of polar residues lining the inner and outer gates. In addition, a high-resolution Cd(2+)-bound structure highlights differences in how Cd(2+) and Mn(2+) are coordinated by DraNramp. Complementary metal binding studies using isothermal titration calorimetry with a series of mutated DraNramp proteins indicate that the thermodynamic landscape for binding and transporting physiological metals like Mn(2+) is different and more robust to perturbation than for transporting the toxic Cd(2+) metal. Overall, the affinity measurements and high-resolution structural information on metal substrate binding provide a foundation for understanding the substrate selectivity of essential metal ion transporters like Nramps. | ||
- | + | High-resolution structures with bound Mn(2+) and Cd(2+) map the metal import pathway in an Nramp transporter.,Ray S, Berry SP, Wilson EA, Zhang CH, Shekhar M, Singharoy A, Gaudet R Elife. 2023 Apr 11;12:e84006. doi: 10.7554/eLife.84006. PMID:37039477<ref>PMID:37039477</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 8e6n" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: Ray | + | </StructureSection> |
+ | [[Category: Deinococcus radiodurans]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Bozzi AT]] | ||
+ | [[Category: Gaudet R]] | ||
+ | [[Category: Nicoludis JM]] | ||
+ | [[Category: Ray S]] | ||
+ | [[Category: Zimanyi CM]] |
Revision as of 07:22, 3 May 2023
X-ray structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter G223W mutant in an outward-open, manganese-bound state
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