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| | <StructureSection load='3ew0' size='340' side='right'caption='[[3ew0]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='3ew0' size='340' side='right'caption='[[3ew0]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ew0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EW0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ew0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EW0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qh7|2qh7]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C10orf70, CISD1, MDS029, ZCD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3ew0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ew0 OCA], [https://pdbe.org/3ew0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ew0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ew0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ew0 ProSAT]</span></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=3ew0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ew0 OCA], [https://pdbe.org/3ew0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ew0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ew0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ew0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CISD1_HUMAN CISD1_HUMAN]] Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions.<ref>PMID:17584744</ref> <ref>PMID:17766440</ref>
| + | [https://www.uniprot.org/uniprot/CISD1_HUMAN CISD1_HUMAN] Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions.<ref>PMID:17584744</ref> <ref>PMID:17766440</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abresch, E C]] | + | [[Category: Abresch EC]] |
| - | [[Category: Axelrod, H L]] | + | [[Category: Axelrod HL]] |
| - | [[Category: Cohen, A E]] | + | [[Category: Cohen AE]] |
| - | [[Category: Conlan, A R]] | + | [[Category: Conlan AR]] |
| - | [[Category: Jennings, P A]] | + | [[Category: Jennings PA]] |
| - | [[Category: Nechushtai, R]] | + | [[Category: Nechushtai R]] |
| - | [[Category: Paddock, M L]] | + | [[Category: Paddock ML]] |
| - | [[Category: Roy, M]] | + | [[Category: Roy M]] |
| - | [[Category: Wiley, S]] | + | [[Category: Wiley S]] |
| - | [[Category: 2fe-2s protein]]
| + | |
| - | [[Category: Highyield expression]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Iron-sulfur]]
| + | |
| - | [[Category: Isotopic labeling]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Mitochondrial outer membrane]]
| + | |
| - | [[Category: Mitochondrion]]
| + | |
| - | [[Category: Mitochondrion outer membrane]]
| + | |
| - | [[Category: Signal-anchor]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
CISD1_HUMAN Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A primary role for mitochondrial dysfunction is indicated in the pathogenesis of insulin resistance. A widely used drug for the treatment of type 2 diabetes is pioglitazone, a member of the thiazolidinedione class of molecules. MitoNEET, a 2Fe-2S outer mitochondrial membrane protein, binds pioglitazone [Colca et al. (2004), Am. J. Physiol. Endocrinol. Metab. 286, E252-E260]. The soluble domain of the human mitoNEET protein has been expressed C-terminal to the superfolder green fluorescent protein and the mitoNEET protein has been isolated. Comparison of the crystal structure of mitoNEET isolated from cleavage of the fusion protein (1.4 A resolution, R factor = 20.2%) with other solved structures shows that the CDGSH domains are superimposable, indicating proper assembly of mitoNEET. Furthermore, there is considerable flexibility in the position of the cytoplasmic tethering arms, resulting in two different conformations in the crystal structure. This flexibility affords multiple orientations on the outer mitochondrial membrane.
The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain.,Conlan AR, Paddock ML, Axelrod HL, Cohen AE, Abresch EC, Wiley S, Roy M, Nechushtai R, Jennings PA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):654-9. Epub, 2009 Jun 27. PMID:19574633[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wiley SE, Paddock ML, Abresch EC, Gross L, van der Geer P, Nechushtai R, Murphy AN, Jennings PA, Dixon JE. The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster. J Biol Chem. 2007 Aug 17;282(33):23745-9. Epub 2007 Jun 21. PMID:17584744 doi:C700107200
- ↑ Paddock ML, Wiley SE, Axelrod HL, Cohen AE, Roy M, Abresch EC, Capraro D, Murphy AN, Nechushtai R, Dixon JE, Jennings PA. MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone. Proc Natl Acad Sci U S A. 2007 Sep 4;104(36):14342-7. Epub 2007 Aug 31. PMID:17766440
- ↑ Conlan AR, Paddock ML, Axelrod HL, Cohen AE, Abresch EC, Wiley S, Roy M, Nechushtai R, Jennings PA. The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):654-9. Epub, 2009 Jun 27. PMID:19574633 doi:10.1107/S1744309109019605
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