2km1

From Proteopedia

(Difference between revisions)

Revision as of 07:28, 14 April 2021

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

Structural highlights

2km1 is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	YKR071C (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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]^[1] ^[2] ^[3] ^[4] ^[5]

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

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chanet R, Heude M. Characterization of mutations that are synthetic lethal with pol3-13, a mutated allele of DNA polymerase delta in Saccharomyces cerevisiae. Curr Genet. 2003 Aug;43(5):337-50. Epub 2003 May 21. PMID:12759774 doi:http://dx.doi.org/10.1007/s00294-003-0407-2
↑ Zhang Y, Lyver ER, Nakamaru-Ogiso E, Yoon H, Amutha B, Lee DW, Bi E, Ohnishi T, Daldal F, Pain D, Dancis A. Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis. Mol Cell Biol. 2008 Sep;28(18):5569-82. doi: 10.1128/MCB.00642-08. Epub 2008 Jul , 14. PMID:18625724 doi:http://dx.doi.org/10.1128/MCB.00642-08
↑ Vernis L, Facca C, Delagoutte E, Soler N, Chanet R, Guiard B, Faye G, Baldacci G. A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast. PLoS One. 2009;4(2):e4376. doi: 10.1371/journal.pone.0004376. Epub 2009 Feb 5. PMID:19194512 doi:http://dx.doi.org/10.1371/journal.pone.0004376
↑ Netz DJ, Stumpfig M, Dore C, Muhlenhoff U, Pierik AJ, Lill R. Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis. Nat Chem Biol. 2010 Oct;6(10):758-65. doi: 10.1038/nchembio.432. Epub 2010 Aug, 29. PMID:20802492 doi:http://dx.doi.org/10.1038/nchembio.432
↑ Soler N, Delagoutte E, Miron S, Facca C, Baille D, d'Autreaux B, Craescu G, Frapart YM, Mansuy D, Baldacci G, Huang ME, Vernis L. Interaction between the reductase Tah18 and highly conserved Fe-S containing Dre2 C-terminus is essential for yeast viability. Mol Microbiol. 2011 Oct;82(1):54-67. doi: 10.1111/j.1365-2958.2011.07788.x. Epub , 2011 Sep 8. PMID:21902732 doi:http://dx.doi.org/10.1111/j.1365-2958.2011.07788.x
↑ Soler N, Craescu CT, Gallay J, Frapart YM, Mansuy D, Raynal B, Baldacci G, Pastore A, Huang ME, Vernis L. A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S containing yeast protein Dre2. FEBS J. 2012 Apr 9. doi: 10.1111/j.1742-4658.2012.08597.x. PMID:22487307 doi:10.1111/j.1742-4658.2012.08597.x

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/2km1"

@@ Line 1: / Line 1: @@
 ==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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2km1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KM1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2km1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YKR071C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YKR071C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2km1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km1 OCA], [http://pdbe.org/2km1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2km1 RCSB], [http://www.ebi.ac.uk/pdbsum/2km1 PDBsum], [http://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>
 == Function ==
-[[http://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>
+[[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Atcc 18824]]
+[[Category: Large Structures]]
 [[Category: Baldacci, G]]
 [[Category: Craescu, C T]]

2km1

From Proteopedia

Revision as of 07:28, 14 April 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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