5m94
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Staphylococcus capitis divalent metal ion transporter (DMT) in complex with nanobody== | |
| + | <StructureSection load='5m94' size='340' side='right' caption='[[5m94]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m94]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M94 FirstGlance]. <br> | ||
| + | </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=5m94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m94 OCA], [http://pdbe.org/5m94 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m94 RCSB], [http://www.ebi.ac.uk/pdbsum/5m94 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m94 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A0S4MEX1_STACP A0A0S4MEX1_STACP]] H(+)-stimulated, divalent metal cation uptake system.[HAMAP-Rule:MF_00221] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Members of the SLC11 (NRAMP) family transport iron and other transition-metal ions across cellular membranes. These membrane proteins are present in all kingdoms of life with a high degree of sequence conservation. To gain insight into the determinants of ion selectivity, we have determined the crystal structure of Staphylococcus capitis DMT (ScaDMT), a close prokaryotic homolog of the family. ScaDMT shows a familiar architecture that was previously identified in the amino acid permease LeuT. The protein adopts an inward-facing conformation with a substrate-binding site located in the center of the transporter. This site is composed of conserved residues, which coordinate Mn2+, Fe2+ and Cd2+ but not Ca2+. Mutations of interacting residues affect ion binding and transport in both ScaDMT and human DMT1. Our study thus reveals a conserved mechanism for transition-metal ion selectivity within the SLC11 family. | ||
| - | + | Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport.,Ehrnstorfer IA, Geertsma ER, Pardon E, Steyaert J, Dutzler R Nat Struct Mol Biol. 2014 Oct 19. doi: 10.1038/nsmb.2904. PMID:25326704<ref>PMID:25326704</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5m94" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Dutzler, R]] | [[Category: Dutzler, R]] | ||
| - | [[Category: Ehrnstorfer, I | + | [[Category: Ehrnstorfer, I A]] |
| + | [[Category: Transition metal ion transporter]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 21:27, 22 December 2016
Crystal structure of Staphylococcus capitis divalent metal ion transporter (DMT) in complex with nanobody
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