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| | <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=2qh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qh7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qh7 RCSB], [http://www.ebi.ac.uk/pdbsum/2qh7 PDBsum]</span></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=2qh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qh7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qh7 RCSB], [http://www.ebi.ac.uk/pdbsum/2qh7 PDBsum]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[http://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]] |
| Line 30: |
Line 32: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Axelrod, H L.]] | + | [[Category: Axelrod, H L]] |
| - | [[Category: Capraro, D.]] | + | [[Category: Capraro, D]] |
| - | [[Category: Cohen, A E.]] | + | [[Category: Cohen, A E]] |
| - | [[Category: Dixon, J E.]] | + | [[Category: Dixon, J E]] |
| - | [[Category: E C., Abresch..]] | + | [[Category: E C., Abresch]] |
| - | [[Category: Jennings, P A.]] | + | [[Category: Jennings, P A]] |
| - | [[Category: Murphy, A N.]] | + | [[Category: Murphy, A N]] |
| - | [[Category: Nechushtai, R.]] | + | [[Category: Nechushtai, R]] |
| - | [[Category: Paddock, M L.]] | + | [[Category: Paddock, M L]] |
| - | [[Category: Roy, M.]] | + | [[Category: Roy, M]] |
| - | [[Category: Wiley, S E.]] | + | [[Category: Wiley, S E]] |
| | [[Category: 2fe-2s protein]] | | [[Category: 2fe-2s protein]] |
| | [[Category: Metal binding protein]] | | [[Category: Metal binding protein]] |
| 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
Iron-sulfur (Fe-S) proteins are key players in vital processes involving energy homeostasis and metabolism from the simplest to most complex organisms. We report a 1.5 A x-ray crystal structure of the first identified outer mitochondrial membrane Fe-S protein, mitoNEET. Two protomers intertwine to form a unique dimeric structure that constitutes a new fold to not only the approximately 650 reported Fe-S protein structures but also to all known proteins. We name this motif the NEET fold. The protomers form a two-domain structure: a beta-cap domain and a cluster-binding domain that coordinates two acid-labile 2Fe-2S clusters. Binding of pioglitazone, an insulin-sensitizing thiazolidinedione used in the treatment of type 2 diabetes, stabilizes the protein against 2Fe-2S cluster release. The biophysical properties of mitoNEET suggest that it may participate in a redox-sensitive signaling and/or in Fe-S cluster transfer.
MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone.,Paddock ML, Wiley SE, Axelrod HL, Cohen AE, Roy M, Abresch EC, Capraro D, Murphy AN, Nechushtai R, Dixon JE, Jennings PA Proc Natl Acad Sci U S A. 2007 Sep 4;104(36):14342-7. Epub 2007 Aug 31. PMID:17766440[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
- ↑ 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
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