5ayo: Difference between revisions

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'''Unreleased structure'''


The entry 5ayo is ON HOLD
==Crystal structure of a bacterial homologue of iron transporter ferroportin in inward-facing state==
 
<StructureSection load='5ayo' size='340' side='right'caption='[[5ayo]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
Authors: Taniguchi, R., Kato, H.E., Font, J., Deshpande, C.N., Ishitani, R., Jormakka, M., Nureki, O.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5ayo]] 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=5AYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AYO FirstGlance]. <br>
Description: Crystal structure of a metal transporter
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Nureki, O]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ayo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ayo OCA], [https://pdbe.org/5ayo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ayo RCSB], [https://www.ebi.ac.uk/pdbsum/5ayo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ayo ProSAT]</span></td></tr>
[[Category: Jormakka, M]]
</table>
[[Category: Kato, H.E]]
== Function ==
[[Category: Taniguchi, R]]
[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>
[[Category: Deshpande, C.N]]
== References ==
[[Category: Ishitani, R]]
<references/>
[[Category: Font, J]]
__TOC__
</StructureSection>
[[Category: Bdellovibrio bacteriovorus HD100]]
[[Category: Large Structures]]
[[Category: Deshpande CN]]
[[Category: Font J]]
[[Category: Ishitani R]]
[[Category: Jormakka M]]
[[Category: Kato HE]]
[[Category: Nureki O]]
[[Category: Taniguchi R]]

Latest revision as of 12:06, 20 March 2024

Crystal structure of a bacterial homologue of iron transporter ferroportin in inward-facing stateCrystal structure of a bacterial homologue of iron transporter ferroportin in inward-facing state

Structural highlights

5ayo 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 3.3Å
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

5ayo, resolution 3.30Å

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