2r13

From Proteopedia

(Difference between revisions)

Revision as of 04:11, 2 July 2021

Crystal structure of human mitoNEET reveals a novel [2Fe-2S] cluster coordination

Structural highlights

2r13 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
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]

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

MitoNEET was identified as an outer mitochondrial membrane protein that can potentially bind the anti-diabetes drug pioglitazone. The crystal structure of the cytoplasmic mitoNEET (residues 33-108) is determined in this study. The structure presents a novel protein fold and contains a [2Fe-2S] cluster-binding domain. The [2Fe-2S] cluster is coordinated to the protein by Cys-72, Cys-74, Cys-83, and His-87 residues. This coordination is also novel compared with the traditional [2Fe-2S] cluster coordinated by four cysteines or two cysteines and two histidines. The cytoplasmic mitoNEET forms homodimers in solution and in crystal. The dimerization is mainly mediated by hydrophobic interactions as well as hydrogen bonds coordinated by two water molecules binding at the interface. His-87 residue, which plays an important role in the coordination of the [2Fe-2S] cluster, is exposed to the solvent on the dimer surface. It is proposed that mitoNEET dimer may interact with other proteins via the surface residues in close proximity to the [2Fe-2S] cluster.

Crystallographic studies of human MitoNEET.,Hou X, Liu R, Ross S, Smart EJ, Zhu H, Gong W J Biol Chem. 2007 Nov 16;282(46):33242-6. Epub 2007 Sep 27. PMID:17905743^[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
↑ Hou X, Liu R, Ross S, Smart EJ, Zhu H, Gong W. Crystallographic studies of human MitoNEET. J Biol Chem. 2007 Nov 16;282(46):33242-6. Epub 2007 Sep 27. PMID:17905743 doi:10.1074/jbc.C700172200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2r13"

@@ Line 3: / Line 3: @@
 <StructureSection load='2r13' size='340' side='right'caption='[[2r13]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2r13]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R13 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R13 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2r13]] is a 1 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=2R13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R13 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></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=2r13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r13 OCA], [http://pdbe.org/2r13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r13 RCSB], [http://www.ebi.ac.uk/pdbsum/2r13 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r13 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=2r13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r13 OCA], [https://pdbe.org/2r13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r13 RCSB], [https://www.ebi.ac.uk/pdbsum/2r13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r13 ProSAT]</span></td></tr>
 </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>
+[[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

2r13

From Proteopedia

Revision as of 04:11, 2 July 2021

Crystal structure of human mitoNEET reveals a novel [2Fe-2S] cluster coordination

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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