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| | ==Solution structure of iron-sulfur cluster assembly protein SUFU from Bacillus subtilis, with zinc bound at the active site. Northeast Structural Genomics Consortium target SR17== | | ==Solution structure of iron-sulfur cluster assembly protein SUFU from Bacillus subtilis, with zinc bound at the active site. Northeast Structural Genomics Consortium target SR17== |
| - | <StructureSection load='2azh' size='340' side='right'caption='[[2azh]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2azh' size='340' side='right'caption='[[2azh]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2azh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AZH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2azh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AZH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xjs|1xjs]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YURV ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=2azh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2azh OCA], [https://pdbe.org/2azh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2azh RCSB], [https://www.ebi.ac.uk/pdbsum/2azh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2azh ProSAT], [https://www.topsan.org/Proteins/NESGC/2azh TOPSAN]</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=2azh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2azh OCA], [https://pdbe.org/2azh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2azh RCSB], [https://www.ebi.ac.uk/pdbsum/2azh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2azh ProSAT], [https://www.topsan.org/Proteins/NESGC/2azh TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SUFU_BACSU SUFU_BACSU]] Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255), but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein (PubMed:24321018). Has been shown to bind low levels of a labile, air-sensitive Fe-S cluster; this can be assembled under anaerobic conditions from FeCl(3) and Li(2)S. Has been shown to be able to transfer this Fe-S cluster to an acceptor protein. Stimulates the cysteine desulfurase activity of SufS, for which it acts as a second substrate. Alkylation eliminates its ability to stimulate SufS. 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:21236255</ref> <ref>PMID:21744456</ref> <ref>PMID:24321018</ref>
| + | [https://www.uniprot.org/uniprot/SUFU_BACSU SUFU_BACSU] Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255), but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein (PubMed:24321018). Has been shown to bind low levels of a labile, air-sensitive Fe-S cluster; this can be assembled under anaerobic conditions from FeCl(3) and Li(2)S. Has been shown to be able to transfer this Fe-S cluster to an acceptor protein. Stimulates the cysteine desulfurase activity of SufS, for which it acts as a second substrate. Alkylation eliminates its ability to stimulate SufS. 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:21236255</ref> <ref>PMID:21744456</ref> <ref>PMID:24321018</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aramini, J M]] | + | [[Category: Aramini JM]] |
| - | [[Category: Cort, J R]] | + | [[Category: Cort JR]] |
| - | [[Category: Kennedy, M A]] | + | [[Category: Kennedy MA]] |
| - | [[Category: Kornhaber, G J]] | + | [[Category: Kornhaber GJ]] |
| - | [[Category: Montelione, G T]] | + | [[Category: Montelione GT]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Ramelot TA]] |
| - | [[Category: Ramelot, T A]] | + | [[Category: Swapna GVT]] |
| - | [[Category: Swapna, G V.T]] | + | |
| - | [[Category: Autostructure]]
| + | |
| - | [[Category: Iron-sulfur]]
| + | |
| - | [[Category: Iscu]]
| + | |
| - | [[Category: Nesg]]
| + | |
| - | [[Category: Nifu-like]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Sr17]]
| + | |
| - | [[Category: Sufu]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| - | [[Category: Zinc]]
| + | |
| Structural highlights
Function
SUFU_BACSU Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255), but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein (PubMed:24321018). Has been shown to bind low levels of a labile, air-sensitive Fe-S cluster; this can be assembled under anaerobic conditions from FeCl(3) and Li(2)S. Has been shown to be able to transfer this Fe-S cluster to an acceptor protein. Stimulates the cysteine desulfurase activity of SufS, for which it acts as a second substrate. Alkylation eliminates its ability to stimulate SufS. 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] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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, Peuckert F, Landmann H, Miethke M, Seubert A, Marahiel MA. Mechanistic characterization of sulfur transfer from cysteine desulfurase SufS to the iron-sulfur scaffold SufU in Bacillus subtilis. FEBS Lett. 2011 Feb 4;585(3):465-70. doi: 10.1016/j.febslet.2011.01.005. Epub, 2011 Jan 12. PMID:21236255 doi:http://dx.doi.org/10.1016/j.febslet.2011.01.005
- ↑ 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
- ↑ Selbach BP, Chung AH, Scott AD, George SJ, Cramer SP, Dos Santos PC. Fe-S cluster biogenesis in Gram-positive bacteria: SufU is a zinc-dependent sulfur transfer protein. Biochemistry. 2014 Jan 14;53(1):152-60. doi: 10.1021/bi4011978. Epub 2013 Dec 23. PMID:24321018 doi:http://dx.doi.org/10.1021/bi4011978
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