2km1
From Proteopedia
(Difference between revisions)
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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 | + | <StructureSection load='2km1' size='340' side='right'caption='[[2km1]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2km1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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> |
| - | </td></tr><tr id=' | + | </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> | <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> | </table> | ||
== Function == | == 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|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2km1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Baldacci | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Craescu | + | [[Category: Baldacci G]] |
| - | [[Category: Delagoutte | + | [[Category: Craescu CT]] |
| - | [[Category: Soler | + | [[Category: Delagoutte E]] |
| - | [[Category: Vernis-Beringue | + | [[Category: Soler N]] |
| - | + | [[Category: Vernis-Beringue L]] | |
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Current revision
Solution structure of the N-terminal domain of the yeast protein Dre2
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