6vyh: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 6vyh is ON HOLD
+==Cryo-EM structure of SLC40/ferroportin in complex with Fab==
+<StructureSection load='6vyh' size='340' side='right'caption='[[6vyh]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6vyh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Carlito_syrichta Carlito syrichta] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VYH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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=6vyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vyh OCA], [https://pdbe.org/6vyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vyh RCSB], [https://www.ebi.ac.uk/pdbsum/6vyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vyh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A1U7U6F1_CARSF A0A1U7U6F1_CARSF] May be involved in iron transport and iron homeostasis.[RuleBase:RU365065]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ferroportin is an iron exporter essential for releasing cellular iron into circulation. Ferroportin is inhibited by a peptide hormone, hepcidin. In humans, mutations in ferroportin lead to ferroportin diseases that are often associated with accumulation of iron in macrophages and symptoms of iron deficiency anemia. Here we present the structures of the ferroportin from the primate Philippine tarsier (TsFpn) in the presence and absence of hepcidin solved by cryo-electron microscopy. TsFpn is composed of two domains resembling a clamshell and the structure defines two metal ion binding sites, one in each domain. Both structures are in an outward-facing conformation, and hepcidin binds between the two domains and reaches one of the ion binding sites. Functional studies show that TsFpn is an electroneutral H(+)/Fe(2+) antiporter so that transport of each Fe(2+) is coupled to transport of two H(+) in the opposite direction. Perturbing either of the ion binding sites compromises the coupled transport of H(+) and Fe(2+). These results establish the structural basis of metal ion binding, transport and inhibition in ferroportin and provide a blueprint for targeting ferroportin in pharmacological intervention of ferroportin diseases.
-Authors:
+Structural basis of ion transport and inhibition in ferroportin.,Pan Y, Ren Z, Gao S, Shen J, Wang L, Xu Z, Yu Y, Bachina P, Zhang H, Fan X, Laganowsky A, Yan N, Zhou M Nat Commun. 2020 Nov 10;11(1):5686. doi: 10.1038/s41467-020-19458-6. PMID:33173040<ref>PMID:33173040</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6vyh" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Carlito syrichta]]
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Gao S]]
+[[Category: Pan Y]]
+[[Category: Ren Z]]
+[[Category: Shen J]]
+[[Category: Yan N]]
+[[Category: Zhou M]]