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| | ==Crystal structure of IscS from Mycobacterium tuberculosis== | | ==Crystal structure of IscS from Mycobacterium tuberculosis== |
| - | <StructureSection load='4isy' size='340' side='right' caption='[[4isy]], [[Resolution|resolution]] 2.59Å' scene=''> | + | <StructureSection load='4isy' size='340' side='right'caption='[[4isy]], [[Resolution|resolution]] 2.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4isy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ISY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ISY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4isy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ISY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ISY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></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=4isy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4isy OCA], [https://pdbe.org/4isy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4isy RCSB], [https://www.ebi.ac.uk/pdbsum/4isy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4isy ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">iscS, MT3109, Rv3025c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4isy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4isy OCA], [http://pdbe.org/4isy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4isy RCSB], [http://www.ebi.ac.uk/pdbsum/4isy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4isy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ISCS_MYCTU ISCS_MYCTU]] Catalyzes the removal of elemental sulfur from cysteine to produce alanine (Probable). Participates in the biosynthesis of metalloclusters by providing the inorganic sulfur required for Fe-S core formation. One acceptor is Whib3, on which this enzyme assembles a 4Fe-4S cluster. | + | [https://www.uniprot.org/uniprot/ISCSL_MYCTU ISCSL_MYCTU] Catalyzes the removal of elemental sulfur from cysteine to produce alanine (Probable). Participates in the biosynthesis of metalloclusters by providing the inorganic sulfur required for Fe-S core formation. One acceptor is Whib3, on which this enzyme assembles a 4Fe-4S cluster. It can use both L-cysteine and L-selenocysteine as substrates.<ref>PMID:17609386</ref> <ref>PMID:24548275</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 4isy" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4isy" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cysteine desulfurase 3D structures|Cysteine desulfurase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cysteine desulfurase]] | + | [[Category: Large Structures]] |
| - | [[Category: Cole, S T]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Pojer, F]] | + | [[Category: Cole ST]] |
| - | [[Category: Rybniker, J]] | + | [[Category: Pojer F]] |
| - | [[Category: Desulfurase]] | + | [[Category: Rybniker J]] |
| - | [[Category: Plp cofactor]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
ISCSL_MYCTU Catalyzes the removal of elemental sulfur from cysteine to produce alanine (Probable). Participates in the biosynthesis of metalloclusters by providing the inorganic sulfur required for Fe-S core formation. One acceptor is Whib3, on which this enzyme assembles a 4Fe-4S cluster. It can use both L-cysteine and L-selenocysteine as substrates.[1] [2]
Publication Abstract from PubMed
The complex multi-protein systems for the assembly of protein-bound Iron-sulfur (Fe-S) clusters are well defined in Gram-negative model organisms. Little is known about Fe-S cluster biogenesis in other bacterial species. The iron-sulfur cluster (ISC) operon of Mycobacterium tuberculosis lacks several genes known to be essential for the function of this system in other organisms. However, the cysteine desulfurase IscSMtb (Rv3025c) is conserved in this important pathogen. This work demonstrates that deleting iscSMtb renders the cells microaerophilic and hypersensitive to oxidative stress. Moreover, the iscSMtb mutant shows impaired Fe-S cluster dependent enzyme activity clearly indicating that IscSMtb is associated with Fe-S cluster assembly. An extensive interaction network of IscSMtb with Fe-S proteins was identified, suggesting a novel mechanism of sulfur transfer by direct interaction with apoproteins. Interestingly, the highly homologous IscS of Escherichia coli failed to complement the iscSMtb mutant and showed a less diverse protein-interaction profile. To identify a structural basis for these observations we determined the crystal structure of IscSMtb, which mirrors adaptations made in response to an ISC-operon devoid of IscU-like Fe-S cluster scaffold proteins. We conclude that in M. tuberculosis IscS has been redesigned during evolution to compensate for the deletion of large parts of the ISC-operon.
The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defense.,Rybniker J, Pojer F, Marienhagen J, Kolly GS, Chen JM, van Gumpel E, Hartmann P, Cole ST Biochem J. 2014 Feb 19. PMID:24548275[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Singh A, Guidry L, Narasimhulu KV, Mai D, Trombley J, Redding KE, Giles GI, Lancaster JR Jr, Steyn AJ. Mycobacterium tuberculosis WhiB3 responds to O2 and nitric oxide via its [4Fe-4S] cluster and is essential for nutrient starvation survival. Proc Natl Acad Sci U S A. 2007 Jul 10;104(28):11562-7. doi:, 10.1073/pnas.0700490104. Epub 2007 Jul 3. PMID:17609386 doi:http://dx.doi.org/10.1073/pnas.0700490104
- ↑ Rybniker J, Pojer F, Marienhagen J, Kolly GS, Chen JM, van Gumpel E, Hartmann P, Cole ST. The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defense. Biochem J. 2014 Feb 19. PMID:24548275 doi:http://dx.doi.org/10.1042/BJ20130732
- ↑ Rybniker J, Pojer F, Marienhagen J, Kolly GS, Chen JM, van Gumpel E, Hartmann P, Cole ST. The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defense. Biochem J. 2014 Feb 19. PMID:24548275 doi:http://dx.doi.org/10.1042/BJ20130732
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