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==Solution structure of the N-terminal domain of the yeast protein Dre2==
==Solution structure of the N-terminal domain of the yeast protein Dre2==
<StructureSection load='2km1' size='340' side='right' caption='[[2km1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2km1' size='340' side='right'caption='[[2km1]]' scene=''>
== Structural highlights ==
== Structural highlights ==
[[2km1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KM1 OCA]. <br>
<table><tr><td colspan='2'>[[2km1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KM1 FirstGlance]. <br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2km1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km1 OCA], [https://pdbe.org/2km1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2km1 RCSB], [https://www.ebi.ac.uk/pdbsum/2km1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2km1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DRE2_YEAST DRE2_YEAST] Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Electrons are transferred to the Fe-S cluster from NADPH via the FAD- and FMN-containing protein TAH18. Has anti-apoptotic effects in the cell. Involved in negative control of H(2)O(2)-induced cell death.[HAMAP-Rule:MF_03115]<ref>PMID:12759774</ref> <ref>PMID:18625724</ref> <ref>PMID:19194512</ref> <ref>PMID:20802492</ref> <ref>PMID:21902732</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/2km1_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/2km1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2km1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== Publication Abstract from PubMed ==
Yeast Dre2 is an essential Fe-S cluster-containing protein that has been implicated in cytosolic Fe-S protein biogenesis and in cell death regulation in response to oxidative stress. Its absence in yeast can be complemented by the human homologous antiapoptotic protein Ciapin1/Anamorsin, suggesting at least one common function. Using complementary techniques, we have investigated the biochemical and biophysical properties of Dre2. We show that it contains an N-terminal domain whose structure in solution consists of a stable well-structured monomer with an overall typical S-adenosylmethionine (SAM) methyltransferase fold that however lacks two alpha helices and a beta strand. The highly conserved C-terminus of Dre2, containing two Fe-S clusters, influences the flexibility of the N-terminal domain. We discuss the hypotheses that the activity of the N-terminal domain could be modulated by the redox activity of Fe-S clusters-containing C-terminus domain in vivo.
A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S containing yeast protein Dre2.,Soler N, Craescu CT, Gallay J, Frapart YM, Mansuy D, Raynal B, Baldacci G, Pastore A, Huang ME, Vernis L FEBS J. 2012 Apr 9. doi: 10.1111/j.1742-4658.2012.08597.x. PMID:22487307<ref>PMID:22487307</ref>
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Baldacci, G.]]
[[Category: Baldacci G]]
[[Category: Craescu, C T.]]
[[Category: Craescu CT]]
[[Category: Delagoutte, E.]]
[[Category: Delagoutte E]]
[[Category: Soler, N.]]
[[Category: Soler N]]
[[Category: Vernis-Beringue, L.]]
[[Category: Vernis-Beringue L]]
[[Category: Antiapoptotic]]
[[Category: Dre2]]
[[Category: Protein binding]]
[[Category: Yeast]]

Latest revision as of 06:46, 1 May 2024

Solution structure of the N-terminal domain of the yeast protein Dre2

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