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| | <StructureSection load='5nq6' size='340' side='right'caption='[[5nq6]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='5nq6' size='340' side='right'caption='[[5nq6]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nq6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NQ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nq6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQ6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ft4|5ft4]], [[5ft5|5ft5]], [[5ft6|5ft6]], [[5ft8|5ft8]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nq6 OCA], [http://pdbe.org/5nq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nq6 RCSB], [http://www.ebi.ac.uk/pdbsum/5nq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nq6 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=5nq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nq6 OCA], [https://pdbe.org/5nq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nq6 RCSB], [https://www.ebi.ac.uk/pdbsum/5nq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nq6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CSDE_ECOLI CSDE_ECOLI]] Stimulates the cysteine desulfurase activity of CsdA. Contains a cysteine residue (Cys-61) that acts to accept sulfur liberated via the desulfurase activity of CsdA. May be able to transfer sulfur to TcdA/CsdL. Seems to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. Does not appear to participate in Fe/S biogenesis.<ref>PMID:15901727</ref> <ref>PMID:20054882</ref> <ref>PMID:23242255</ref> | + | [https://www.uniprot.org/uniprot/CSDE_ECOLI CSDE_ECOLI] Stimulates the cysteine desulfurase activity of CsdA. Contains a cysteine residue (Cys-61) that acts to accept sulfur liberated via the desulfurase activity of CsdA. May be able to transfer sulfur to TcdA/CsdL. Seems to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. Does not appear to participate in Fe/S biogenesis.<ref>PMID:15901727</ref> <ref>PMID:20054882</ref> <ref>PMID:23242255</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aranda, J]] | + | [[Category: Aranda J]] |
| - | [[Category: Coll, M]] | + | [[Category: Coll M]] |
| - | [[Category: Fernandez, F J]] | + | [[Category: Fernandez FJ]] |
| - | [[Category: Garces, F]] | + | [[Category: Garces F]] |
| - | [[Category: Gomez, S]] | + | [[Category: Gomez S]] |
| - | [[Category: Lopez-Estepa, M]] | + | [[Category: Lopez-Estepa M]] |
| - | [[Category: Penya-Soler, E]] | + | [[Category: Penya-Soler E]] |
| - | [[Category: Vega, M C]] | + | [[Category: Vega MC]] |
| - | [[Category: L-cysteine desulfurase]]
| + | |
| - | [[Category: Sulfur trafficking]]
| + | |
| - | [[Category: Sulfur-acceptor protein]]
| + | |
| - | [[Category: Sulfur-binding protein]]
| + | |
| - | [[Category: Transpersulfuration]]
| + | |
| Structural highlights
Function
CSDE_ECOLI Stimulates the cysteine desulfurase activity of CsdA. Contains a cysteine residue (Cys-61) that acts to accept sulfur liberated via the desulfurase activity of CsdA. May be able to transfer sulfur to TcdA/CsdL. Seems to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. Does not appear to participate in Fe/S biogenesis.[1] [2] [3]
Publication Abstract from PubMed
Sulfur trafficking in living organisms relies on transpersulfuration reactions consisting in the enzyme-catalyzed transfer of S atoms via activated persulfidic S across protein-protein interfaces. The recent elucidation of the mechanistic basis for transpersulfuration in the CsdA-CsdE model system has paved the way for a better understanding of its role under oxidative stress. Herein we present the crystal structure of the oxidized, inactivated CsdE dimer at 2.4 A resolution. The structure sheds light into the activation of the Cys61 nucleophile on its way from a solvent-secluded position in free CsdE to a fully extended conformation in the persulfurated CsdA-CsdE complex. Molecular dynamics simulations of available CsdE structures allow to delineate the sequence of conformational changes underwent by CsdE and to pinpoint the key role played by the deprotonation of the Cys61 thiol. The low-energy subunit orientation in the disulfide-bridged CsdE dimer demonstrates the likely physiologic relevance of this oxidative dead-end form of CsdE, suggesting that CsdE could act as a redox sensor in vivo.
Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE.,Pena-Soler E, Aranda J, Lopez-Estepa M, Gomez S, Garces F, Coll M, Fernandez FJ, Tunon I, Vega MC PLoS One. 2017 Oct 18;12(10):e0186286. doi: 10.1371/journal.pone.0186286., eCollection 2017. PMID:29045454[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Loiseau L, Ollagnier-de Choudens S, Lascoux D, Forest E, Fontecave M, Barras F. Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli. J Biol Chem. 2005 Jul 22;280(29):26760-9. Epub 2005 May 18. PMID:15901727 doi:http://dx.doi.org/10.1074/jbc.M504067200
- ↑ Trotter V, Vinella D, Loiseau L, Ollagnier de Choudens S, Fontecave M, Barras F. The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein. Mol Microbiol. 2009 Dec;74(6):1527-42. PMID:20054882
- ↑ Miyauchi K, Kimura S, Suzuki T. A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification. Nat Chem Biol. 2013 Feb;9(2):105-11. doi: 10.1038/nchembio.1137. Epub 2012 Dec, 16. PMID:23242255 doi:http://dx.doi.org/10.1038/nchembio.1137
- ↑ Pena-Soler E, Aranda J, Lopez-Estepa M, Gomez S, Garces F, Coll M, Fernandez FJ, Tunon I, Vega MC. Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE. PLoS One. 2017 Oct 18;12(10):e0186286. doi: 10.1371/journal.pone.0186286., eCollection 2017. PMID:29045454 doi:http://dx.doi.org/10.1371/journal.pone.0186286
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