3ree: Difference between revisions

Latest revision as of 10:11, 13 August 2026

Crystal structure of mitoNEET

Structural highlights

3ree is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.76Å
Ligands:	FES
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

Binding of the thiazolidinedione antidiabetic drug pioglitazone led to the discovery of a novel outer mitochondrial membrane protein of unknown function called mitoNEET. The protein is homodimeric and contains a uniquely ligated two iron-two sulfur cluster in each of its two cytosolic domains. Electrospray ionization mass spectrometry was employed to characterize solutions of the soluble cytosolic domain (amino acids 32-108) of the protein. Ions characteristic of dimers containing the cofactors were readily detected under native conditions. mitoNEET responded to exposure to solutions at low pH by dissociation to give monomers that retained the cofactor, followed by dissociation of the cofactor in a concerted fashion. mitoNEET formed complexes with resveratrol-3-sulfate, one of the primary metabolites of the natural product resveratrol. Resveratrol itself showed no tendency to interact with mitoNEET. The formation of complexes was evident in both electrospray ionization mass spectrometry and isothermal titration calorimetry measurements. Up to eight molecules of the compound associated with the dimeric form of the protein in a sequential fashion. Dissociation constants determined by micorcalorimetry were in the range 5-16 muM for the various binding sites. The only other known naturally ocurring binding partner for mitoNEET at present is NADPH. It is very interesting that the iron-sulfur cluster containing protein interacts with two potentially redox active substances at the surface of mitochondria. These findings provide a new direction for research into two poorly understood, yet biomedically relevant species.

Complexes of the Outer Mitochondrial Membrane Protein mitoNEET with Resveratrol-3-sulfate.,Arif W, Xu S, Isailovic D, Geldenhuys WJ, Carroll RT, Funk MO Biochemistry. 2011 May 17. PMID:21591687^[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
↑ Arif W, Xu S, Isailovic D, Geldenhuys WJ, Carroll RT, Funk MO. Complexes of the Outer Mitochondrial Membrane Protein mitoNEET with Resveratrol-3-sulfate. Biochemistry. 2011 May 17. PMID:21591687 doi:10.1021/bi200546s

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] Arif W, Xu S, Isailovic D, Geldenhuys WJ, Carroll RT, Funk MO. Complexes of the Outer Mitochondrial Membrane Protein mitoNEET with Resveratrol-3-sulfate. Biochemistry. 2011 May 17. PMID:21591687 doi:10.1021/bi200546s

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-[[Image:3ree.jpg|left|200px]]
-<!--
+==Crystal structure of mitoNEET==
-The line below this paragraph, containing "STRUCTURE_3ree", creates the "Structure Box" on the page.
+<StructureSection load='3ree' size='340' side='right'caption='[[3ree]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3ree]] is a 1 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=3REE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3REE FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</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>
-{{STRUCTURE_3ree|  PDB=3ree  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ree FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ree OCA], [https://pdbe.org/3ree PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ree RCSB], [https://www.ebi.ac.uk/pdbsum/3ree PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ree ProSAT]</span></td></tr>
+</table>
+== 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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Binding of the thiazolidinedione antidiabetic drug pioglitazone led to the discovery of a novel outer mitochondrial membrane protein of unknown function called mitoNEET. The protein is homodimeric and contains a uniquely ligated two iron-two sulfur cluster in each of its two cytosolic domains. Electrospray ionization mass spectrometry was employed to characterize solutions of the soluble cytosolic domain (amino acids 32-108) of the protein. Ions characteristic of dimers containing the cofactors were readily detected under native conditions. mitoNEET responded to exposure to solutions at low pH by dissociation to give monomers that retained the cofactor, followed by dissociation of the cofactor in a concerted fashion. mitoNEET formed complexes with resveratrol-3-sulfate, one of the primary metabolites of the natural product resveratrol. Resveratrol itself showed no tendency to interact with mitoNEET. The formation of complexes was evident in both electrospray ionization mass spectrometry and isothermal titration calorimetry measurements. Up to eight molecules of the compound associated with the dimeric form of the protein in a sequential fashion. Dissociation constants determined by micorcalorimetry were in the range 5-16 muM for the various binding sites. The only other known naturally ocurring binding partner for mitoNEET at present is NADPH. It is very interesting that the iron-sulfur cluster containing protein interacts with two potentially redox active substances at the surface of mitochondria. These findings provide a new direction for research into two poorly understood, yet biomedically relevant species.
-===Crystal structure of mitoNEET===
+Complexes of the Outer Mitochondrial Membrane Protein mitoNEET with Resveratrol-3-sulfate.,Arif W, Xu S, Isailovic D, Geldenhuys WJ, Carroll RT, Funk MO Biochemistry. 2011 May 17. PMID:21591687<ref>PMID:21591687</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-[[3ree]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3REE OCA].
+<div class="pdbe-citations 3ree" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Arif, W.]]
+[[Category: Large Structures]]
-[[Category: Funk, M O.]]
+[[Category: Arif W]]
-[[Category: Mueser, T C.]]
+[[Category: Funk MO]]
-[[Category: Xu, S.]]
+[[Category: Mueser TC]]
+[[Category: Xu S]]

3ree: Difference between revisions

Latest revision as of 10:11, 13 August 2026

Crystal structure of mitoNEET

Structural highlights

Function

Publication Abstract from PubMed

References

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