This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6d91
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6d91' size='340' side='right' caption='[[6d91]], [[Resolution|resolution]] 2.36Å' scene=''> | <StructureSection load='6d91' size='340' side='right' caption='[[6d91]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6d91]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D91 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d91]] 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=6D91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D91 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | ||
| + | <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> | ||
<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=6d91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d91 OCA], [http://pdbe.org/6d91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d91 RCSB], [http://www.ebi.ac.uk/pdbsum/6d91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d91 ProSAT]</span></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=6d91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d91 OCA], [http://pdbe.org/6d91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d91 RCSB], [http://www.ebi.ac.uk/pdbsum/6d91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d91 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MNTH_DEIRA MNTH_DEIRA]] H(+)-stimulated, divalent metal cation uptake system. | [[http://www.uniprot.org/uniprot/MNTH_DEIRA MNTH_DEIRA]] H(+)-stimulated, divalent metal cation uptake system. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6d91" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Deira]] | ||
[[Category: Bozzi, A T]] | [[Category: Bozzi, A T]] | ||
[[Category: Gaudet, R]] | [[Category: Gaudet, R]] | ||
Revision as of 08:35, 21 February 2019
Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter in the outward-open, apo conformation
| |||||||||||
