6btx: Difference between revisions

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==Structure of a bacterial metal transporter==
==Structure of a bacterial metal transporter==
<StructureSection load='6btx' size='340' side='right' caption='[[6btx]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='6btx' size='340' side='right'caption='[[6btx]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6btx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BTX FirstGlance]. <br>
<table><tr><td colspan='2'>[[6btx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus_HD100 Bdellovibrio bacteriovorus HD100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BTX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDT:{[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC+ACID'>EDT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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=6btx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6btx OCA], [http://pdbe.org/6btx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6btx RCSB], [http://www.ebi.ac.uk/pdbsum/6btx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6btx ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDT:{[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC+ACID'>EDT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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=6btx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6btx OCA], [https://pdbe.org/6btx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6btx RCSB], [https://www.ebi.ac.uk/pdbsum/6btx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6btx ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/FPN_BDEBA FPN_BDEBA] Iron transpoter that exports Fe(2+) from the cell. Also binds to Co(2+) and Ni(2+). May act as a multivalent divalent metal transporter (PubMed:26608034). The transporter is composed of 12 transmembrane (TM) helices organized into N-terminal (TM1-6) and C-terminal (TM7-12) domains. The substrate-binding site is formed at the interface of the two domains and is alternately accessible from either side of the membrane. The transport cycle is viewed as a series of ligand-induced conformational changes that include open outward and open inward states (PubMed:26461048, PubMed:30082682).<ref>PMID:26461048</ref> <ref>PMID:26608034</ref> <ref>PMID:30082682</ref>  
Ferroportin (Fpn)-the only known cellular iron exporter-transports dietary and recycled iron into the blood plasma, and transfers iron across the placenta. Despite its central role in iron metabolism, our molecular understanding of Fpn-mediated iron efflux remains incomplete. Here, we report that Ca(2+) is required for human Fpn transport activity. Whereas iron efflux is stimulated by extracellular Ca(2+) in the physiological range, Ca(2+) is not transported. We determine the crystal structure of a Ca(2+)-bound BbFpn, a prokaryotic orthologue, and find that Ca(2+) is a cofactor that facilitates a conformational change critical to the transport cycle. We also identify a substrate pocket accommodating a divalent transition metal complexed with a chelator. These findings support a model of iron export by Fpn and suggest a link between plasma calcium and iron homeostasis.
 
Calcium is an essential cofactor for metal efflux by the ferroportin transporter family.,Deshpande CN, Ruwe TA, Shawki A, Xin V, Vieth KR, Valore EV, Qiao B, Ganz T, Nemeth E, Mackenzie B, Jormakka M Nat Commun. 2018 Aug 6;9(1):3075. doi: 10.1038/s41467-018-05446-4. PMID:30082682<ref>PMID:30082682</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6btx" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Deshpande, C N]]
[[Category: Bdellovibrio bacteriovorus HD100]]
[[Category: Jormakka, M]]
[[Category: Large Structures]]
[[Category: Metal transport]]
[[Category: Deshpande CN]]
[[Category: Metal transporter]]
[[Category: Jormakka M]]

Latest revision as of 17:24, 13 March 2024

Structure of a bacterial metal transporterStructure of a bacterial metal transporter

Structural highlights

6btx is a 1 chain structure with sequence from Bdellovibrio bacteriovorus HD100. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FPN_BDEBA Iron transpoter that exports Fe(2+) from the cell. Also binds to Co(2+) and Ni(2+). May act as a multivalent divalent metal transporter (PubMed:26608034). The transporter is composed of 12 transmembrane (TM) helices organized into N-terminal (TM1-6) and C-terminal (TM7-12) domains. The substrate-binding site is formed at the interface of the two domains and is alternately accessible from either side of the membrane. The transport cycle is viewed as a series of ligand-induced conformational changes that include open outward and open inward states (PubMed:26461048, PubMed:30082682).[1] [2] [3]

References

  1. ↑ Taniguchi R, Kato HE, Font J, Deshpande CN, Wada M, Ito K, Ishitani R, Jormakka M, Nureki O. Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin. Nat Commun. 2015 Oct 13;6:8545. doi: 10.1038/ncomms9545. PMID:26461048 doi:http://dx.doi.org/10.1038/ncomms9545
  2. ↑ Bonaccorsi di Patti MC, Polticelli F, Tortosa V, Furbetta PA, Musci G. A bacterial homologue of the human iron exporter ferroportin. FEBS Lett. 2015 Dec 21;589(24 Pt B):3829-35. PMID:26608034 doi:10.1016/j.febslet.2015.11.025
  3. ↑ Deshpande CN, Ruwe TA, Shawki A, Xin V, Vieth KR, Valore EV, Qiao B, Ganz T, Nemeth E, Mackenzie B, Jormakka M. Calcium is an essential cofactor for metal efflux by the ferroportin transporter family. Nat Commun. 2018 Aug 6;9(1):3075. doi: 10.1038/s41467-018-05446-4. PMID:30082682 doi:http://dx.doi.org/10.1038/s41467-018-05446-4

6btx, resolution 3.20Å

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