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4ooa

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==CRYSTAL STRUCTURE of NAF1 (MINER1): H114C THE REDOX-ACTIVE 2FE-2S PROTEIN==
==CRYSTAL STRUCTURE of NAF1 (MINER1): H114C THE REDOX-ACTIVE 2FE-2S PROTEIN==
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<StructureSection load='4ooa' size='340' side='right' caption='[[4ooa]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
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<StructureSection load='4ooa' size='340' side='right'caption='[[4ooa]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ooa]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OOA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OOA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ooa]] is a 6 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=4OOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OOA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oo7|4oo7]]</td></tr>
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<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>
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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=4ooa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ooa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ooa RCSB], [http://www.ebi.ac.uk/pdbsum/4ooa PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ooa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ooa OCA], [https://pdbe.org/4ooa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ooa RCSB], [https://www.ebi.ac.uk/pdbsum/4ooa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ooa ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/CISD2_HUMAN CISD2_HUMAN]] Defects in CISD2 are the cause of Wolfram syndrome type 2 (WFS2) [MIM:[http://omim.org/entry/604928 604928]]. A rare disorder characterized by juvenile-onset insulin-dependent diabetes mellitus with optic atrophy. Other manifestations include diabetes insipidus, sensorineural deafness, dementia, psychiatric illnesses. WFS2 patients additionally show a strong bleeding tendency and gastrointestinal ulceration. Diabetes insipidus may be absent.<ref>PMID:17846994</ref>
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[https://www.uniprot.org/uniprot/CISD2_HUMAN CISD2_HUMAN] Defects in CISD2 are the cause of Wolfram syndrome type 2 (WFS2) [MIM:[https://omim.org/entry/604928 604928]. A rare disorder characterized by juvenile-onset insulin-dependent diabetes mellitus with optic atrophy. Other manifestations include diabetes insipidus, sensorineural deafness, dementia, psychiatric illnesses. WFS2 patients additionally show a strong bleeding tendency and gastrointestinal ulceration. Diabetes insipidus may be absent.<ref>PMID:17846994</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CISD2_HUMAN CISD2_HUMAN]] Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it is not involved in BIK-dependent activation of caspases. Involved in life span control, probably via its function as regulator of autophagy.<ref>PMID:17846994</ref> <ref>PMID:20010695</ref>
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[https://www.uniprot.org/uniprot/CISD2_HUMAN CISD2_HUMAN] Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it is not involved in BIK-dependent activation of caspases. Involved in life span control, probably via its function as regulator of autophagy.<ref>PMID:17846994</ref> <ref>PMID:20010695</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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NAF-1 is an important [2Fe-2S] NEET protein associated with human health and disease. A mis-splicing mutation in NAF-1 results in Wolfram Syndrome type 2, a lethal childhood disease. Upregulation of NAF-1 is found in epithelial breast cancer cells, and suppression of NAF-1 expression by knockdown significantly suppresses tumor growth. Key to NAF-1 function is the NEET fold with its [2Fe-2S] cluster. In this work, the high-resolution structure of native NAF-1 was determined to 1.65 A resolution (R factor = 13.5%) together with that of a mutant in which the single His ligand of its [2Fe-2S] cluster, His114, was replaced by Cys. The NAF-1 H114C mutant structure was determined to 1.58 A resolution (R factor = 16.0%). All structural differences were localized to the cluster binding site. Compared with native NAF-1, the [2Fe-2S] clusters of the H114C mutant were found to (i) be 25-fold more stable, (ii) have a redox potential that is 300 mV more negative and (iii) have their cluster donation/transfer function abolished. Because no global structural differences were found between the mutant and the native (wild-type) NAF-1 proteins, yet significant functional differences exist between them, the NAF-1 H114C mutant is an excellent tool to decipher the underlying biological importance of the [2Fe-2S] cluster of NAF-1 in vivo.
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A point mutation in the [2Fe-2S] cluster binding region of the NAF-1 protein (H114C) dramatically hinders the cluster donor properties.,Tamir S, Eisenberg-Domovich Y, Conlan AR, Stofleth JT, Lipper CH, Paddock ML, Mittler R, Jennings PA, Livnah O, Nechushtai R Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1572-8. doi:, 10.1107/S1399004714005458. Epub 2014 May 23. PMID:24914968<ref>PMID:24914968</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Conlan, A R]]
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[[Category: Homo sapiens]]
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[[Category: Eisenberg-Domovich, Y]]
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[[Category: Large Structures]]
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[[Category: Jennings, P A]]
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[[Category: Conlan AR]]
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[[Category: Lipper, C H]]
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[[Category: Eisenberg-Domovich Y]]
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[[Category: Livnah, O]]
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[[Category: Jennings PA]]
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[[Category: Mittler, R]]
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[[Category: Lipper CH]]
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[[Category: Nechushtai, R]]
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[[Category: Livnah O]]
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[[Category: Paddock, M L]]
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[[Category: Mittler R]]
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[[Category: Stofleth, J T]]
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[[Category: Nechushtai R]]
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[[Category: Tamir, S]]
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[[Category: Paddock ML]]
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[[Category: Membrane bound]]
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[[Category: Stofleth JT]]
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[[Category: Metal binding protein]]
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[[Category: Tamir S]]
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[[Category: Oxidative stress]]
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[[Category: Thiazolidinedione]]
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Current revision

CRYSTAL STRUCTURE of NAF1 (MINER1): H114C THE REDOX-ACTIVE 2FE-2S PROTEIN

PDB ID 4ooa

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