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| - | ==Crystal structure of Staphylococcus capitis divalent metal ion transporter (DMT) in complex with nanobody==
| + | #REDIRECT [[5m94]] This PDB entry is obsolete and replaced by 5m94 |
| - | <StructureSection load='4wgv' size='340' side='right' caption='[[4wgv]], [[Resolution|resolution]] 3.10Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4wgv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WGV FirstGlance]. <br>
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| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wgw|4wgw]]</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=4wgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wgv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wgv RCSB], [http://www.ebi.ac.uk/pdbsum/4wgv PDBsum]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/F9L8R0_STACP F9L8R0_STACP]] H(+)-stimulated, divalent metal cation uptake system.[HAMAP-Rule:MF_00221]
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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>
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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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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Dutzler, R]]
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| - | [[Category: Ehrnstorfer, I A]]
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| - | [[Category: Geertsma, E R]]
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| - | [[Category: Pardon, E]]
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| - | [[Category: Steyaert, J]]
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| - | [[Category: Dmt]]
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| - | [[Category: Leut fold]]
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| - | [[Category: Membrane protein]]
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| - | [[Category: Nramp]]
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| - | [[Category: Slc11]]
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| - | [[Category: Transition-metal ion]]
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| - | [[Category: Transport protein]]
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| - | [[Category: Transporter]]
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