2r13

<StructureSection load='2r13' size='340' side='right' caption='[[2r13]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<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>

</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>

<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]</span></td></tr>

[[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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r1/2r13_consurf.spt"</scriptWhenChecked>

<div style="background-color:#fffaf0;">

== 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<ref>PMID:17905743</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2r13" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Gong, W]]

[[Category: Hou, X]]

[[Category: Liu, R]]

[[Category: Ross, S]]

[[Category: Smart, E J]]

[[Category: Zhu, H]]

[[Category: Zinc-finger]]