1xjs: Difference between revisions

Revision as of 10:02, 6 January 2021

Solution structure of Iron-Sulfur cluster assembly protein IscU from Bacillus subtilis, with Zinc bound at the active site. Northeast Structural Genomics Consortium Target SR17

Structural highlights

1xjs is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ZN
Gene:	nifU ("Vibrio subtilis" Ehrenberg 1835)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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:https://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:https://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:https://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:https://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:https://dx.doi.org/10.1021/bi4011978

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OCA

[1] 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:https://dx.doi.org/10.1128/JB.01536-09

[2] 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:https://dx.doi.org/10.1021/bi101358k

[3] 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:https://dx.doi.org/10.1016/j.febslet.2011.01.005

[4] 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:https://dx.doi.org/10.1002/cbic.201100190

[5] 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:https://dx.doi.org/10.1021/bi4011978

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[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
 ==Solution structure of Iron-Sulfur cluster assembly protein IscU from Bacillus subtilis, with Zinc bound at the active site. Northeast Structural Genomics Consortium Target SR17==
-<StructureSection load='1xjs' size='340' side='right' caption='[[1xjs]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1xjs' size='340' side='right'caption='[[1xjs]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xjs]] is a 1 chain structure with sequence from [http://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=1XJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XJS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xjs]] is a 1 chain structure with sequence from [http://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=1XJS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XJS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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">nifU ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjs OCA], [http://pdbe.org/1xjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xjs RCSB], [http://www.ebi.ac.uk/pdbsum/1xjs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xjs ProSAT], [http://www.topsan.org/Proteins/NESGC/1xjs TOPSAN]</span></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=1xjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjs OCA], [http://pdbe.org/1xjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xjs RCSB], [http://www.ebi.ac.uk/pdbsum/1xjs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xjs ProSAT], [http://www.topsan.org/Proteins/NESGC/1xjs TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 </StructureSection>
 [[Category: Vibrio subtilis ehrenberg 1835]]
+[[Category: Large Structures]]
 [[Category: Cort, J R]]
 [[Category: Kennedy, M A]]

1xjs: Difference between revisions

Revision as of 10:02, 6 January 2021

Solution structure of Iron-Sulfur cluster assembly protein IscU from Bacillus subtilis, with Zinc bound at the active site. Northeast Structural Genomics Consortium Target SR17

Structural highlights

Function

Evolutionary Conservation

References

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