5aym: Difference between revisions

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'''Unreleased structure'''


The entry 5aym is ON HOLD
==Crystal structure of a bacterial homologue of iron transporter ferroportin in outward-facing state with soaked iron==
 
<StructureSection load='5aym' size='340' side='right'caption='[[5aym]], [[Resolution|resolution]] 3.00&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'>[[5aym]] 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=5AYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AYM FirstGlance]. <br>
Description:  
</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&#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=FE2:FE+(II)+ION'>FE2</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=5aym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aym OCA], [https://pdbe.org/5aym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aym RCSB], [https://www.ebi.ac.uk/pdbsum/5aym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aym 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]]