Cysteine desulfurase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Cysteine desulfurase''' ( | + | '''Cysteine desulfurase''' (Suf) catalyzes the conversion of L-cysteine to L-alanine and sulfane sulfur. Suf is part of the iron-sulfur cluster complex where '''SufS''' transfers the sulphide from Cys to '''SufU''' which is a scaffold protein<ref>PMID:21236255</ref>. In ''E. coli'', '''SufE''' stimulates the activity of SufS<ref>PMID:12941942</ref>. Suf has a role in the biosynthesis of Fe-S custers, thiamine, thionucleosides, biotin, lipoic acid, molybdopterin and NAD<ref>PMID:12382038</ref>. Suf is a PLP-dependent enzyme. |
== Structural highlights == | == Structural highlights == | ||
| - | The structure of | + | The structure of SufS contains the <scene name='80/800705/Cv/2'>cofactor PLP bound to Lys224</scene>. |
*<scene name='80/800705/Cv/4'>All interactions of PLP</scene>. | *<scene name='80/800705/Cv/4'>All interactions of PLP</scene>. | ||
<scene name='80/800705/Cv/5'>Cys361 is the nucleophilic catalytic residue</scene>. The reaction product <scene name='80/800705/Cv/6'>alanine is bound near the Cys361-persulfide</scene><ref>PMID:27382962</ref>. | <scene name='80/800705/Cv/5'>Cys361 is the nucleophilic catalytic residue</scene>. The reaction product <scene name='80/800705/Cv/6'>alanine is bound near the Cys361-persulfide</scene><ref>PMID:27382962</ref>. | ||
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| - | </StructureSection> | ||
==3D structures of cysteine desulfurase== | ==3D structures of cysteine desulfurase== | ||
| + | [[Cysteine desulfurase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | *Cysteine desulfurase complexes containing cysteine | ||
| - | **[[5j8q]] - BsSUFS + mercaptocysteine + PLP + alanine <br /> | ||
| - | **[[5xt6]] - BsSUFS + SufU + mercaptocysteine + PLP derivative <br /> | ||
| - | **[[4q75]] - AtSUFS 2 + mercaptocysteine + PLP derivative - ''Arabidopsis thaliana''<br /> | ||
| - | **[[5b7u]] - ToSUFS + mercaptocysteine + PLP derivative + cysteine<br /> | ||
| - | **[[5b87]], [[5b89]] - ToSUFS + mercaptocysteine + PLP + alanine<br /> | ||
| - | **[[5ft5]] - EcSUFS CsdA + mercaptocysteine + PLP <br /> | ||
| - | **[[5ft6]] - EcSUFS CsdA + cysteine sulfonic acid + PLP <br /> | ||
| - | **[[5ft8]] - EcSUFS CsdA + sulfur acceptor protein + mercaptocysteine + PLP <br /> | ||
| - | **[[5db5]] - EcSUFS + mercaptocysteine + PLP + cysteine<br /> | ||
| - | **[[5wt4]] - HpSUFS IscS (mutant) + PLP derivative + cysteine derivative - ''Helicobacter pylori''<br /> | ||
| - | **[[5wt6]] - HpSUFS IscS + mercaptocysteine + PLP derivative <br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
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References
- ↑ 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
- ↑ Outten FW, Wood MJ, Munoz FM, Storz G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem. 2003 Nov 14;278(46):45713-9. Epub 2003 Aug 26. PMID:12941942 doi:http://dx.doi.org/10.1074/jbc.M308004200
- ↑ Mihara H, Esaki N. Bacterial cysteine desulfurases: their function and mechanisms. Appl Microbiol Biotechnol. 2002 Oct;60(1-2):12-23. doi:, 10.1007/s00253-002-1107-4. Epub 2002 Sep 4. PMID:12382038 doi:http://dx.doi.org/10.1007/s00253-002-1107-4
- ↑ 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
