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| | ==Crystal Structure of the Cysteine Desulfurase SufS of Bacillus subtilis== | | ==Crystal Structure of the Cysteine Desulfurase SufS of Bacillus subtilis== |
| - | <StructureSection load='5j8q' size='340' side='right' caption='[[5j8q]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5j8q' size='340' side='right'caption='[[5j8q]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5j8q]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J8Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j8q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J8Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 1.702Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_desulfurase Cysteine desulfurase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.7 2.8.1.7] </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=5j8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8q OCA], [https://pdbe.org/5j8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j8q RCSB], [https://www.ebi.ac.uk/pdbsum/5j8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8q ProSAT]</span></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=5j8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8q OCA], [http://pdbe.org/5j8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j8q RCSB], [http://www.ebi.ac.uk/pdbsum/5j8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUFS_BACSU SUFS_BACSU]] Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.<ref>PMID:20097860</ref> <ref>PMID:20822158</ref> <ref>PMID:21744456</ref> | + | [https://www.uniprot.org/uniprot/SUFS_BACSU SUFS_BACSU] Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.<ref>PMID:20097860</ref> <ref>PMID:20822158</ref> <ref>PMID:21744456</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5j8q" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5j8q" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cysteine desulfurase|Cysteine desulfurase]] |
| | + | *[[Cysteine desulfurase 3D structures|Cysteine desulfurase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cysteine desulfurase]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Altegoer, F]] | + | [[Category: Large Structures]] |
| - | [[Category: Bange, G]] | + | [[Category: Altegoer F]] |
| - | [[Category: Iron sulfur cluster]] | + | [[Category: Bange G]] |
| - | [[Category: Suf-system]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
SUFS_BACSU Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.[1] [2] [3]
Publication Abstract from PubMed
The biosynthesis of iron sulfur (Fe-S) clusters in Bacillus subtilis is mediated by a SUF-type gene cluster, consisting of the cysteine desulfurase SufS, the scaffold protein SufU, and the putative chaperone complex SufB/SufC/SufD. Here, we present the high-resolution crystal structure of the SufS homodimer in its product-bound state (i.e., in complex with pyrodoxal-5'-phosphate, alanine, Cys361-persulfide). By performing hydrogen/deuterium exchange (H/DX) experiments, we characterized the interaction of SufS with SufU and demonstrate that SufU induces an opening of the active site pocket of SufS. Recent data indicate that frataxin could be involved in Fe-S cluster biosynthesis by facilitating iron incorporation. H/DX experiments show that frataxin indeed interacts with the SufS/SufU complex at the active site. Our findings deepen the current understanding of Fe-S cluster biosynthesis, a complex yet essential process, in the model organism B. subtilis.
Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU.,Blauenburg B, Mielcarek A, Altegoer F, Fage CD, Linne U, Bange G, Marahiel MA PLoS One. 2016 Jul 6;11(7):e0158749. doi: 10.1371/journal.pone.0158749., eCollection 2016. PMID:27382962[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Albrecht AG, Netz DJ, Miethke M, Pierik AJ, Burghaus O, Peuckert F, Lill R, Marahiel MA. SufU is an essential iron-sulfur cluster scaffold protein in Bacillus subtilis. J Bacteriol. 2010 Mar;192(6):1643-51. doi: 10.1128/JB.01536-09. Epub 2010 Jan 22. PMID:20097860 doi:http://dx.doi.org/10.1128/JB.01536-09
- ↑ Selbach B, Earles E, Dos Santos PC. Kinetic analysis of the bisubstrate cysteine desulfurase SufS from Bacillus subtilis. Biochemistry. 2010 Oct 12;49(40):8794-802. doi: 10.1021/bi101358k. Epub 2010 Sep , 16. PMID:20822158 doi:http://dx.doi.org/10.1021/bi101358k
- ↑ Albrecht AG, Landmann H, Nette D, Burghaus O, Peuckert F, Seubert A, Miethke M, Marahiel MA. The frataxin homologue Fra plays a key role in intracellular iron channeling in Bacillus subtilis. Chembiochem. 2011 Sep 5;12(13):2052-61. doi: 10.1002/cbic.201100190. Epub 2011, Jul 8. PMID:21744456 doi:http://dx.doi.org/10.1002/cbic.201100190
- ↑ Blauenburg B, Mielcarek A, Altegoer F, Fage CD, Linne U, Bange G, Marahiel MA. Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU. PLoS One. 2016 Jul 6;11(7):e0158749. doi: 10.1371/journal.pone.0158749., eCollection 2016. PMID:27382962 doi:http://dx.doi.org/10.1371/journal.pone.0158749
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