Cysteine desulfurase
From Proteopedia
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| - | <StructureSection load='5j8q' size='340' side='right' caption=' | + | <StructureSection load='5j8q' size='340' side='right' caption='Bacterial cysteine desulfurase complex with PLP, mercaptocysteine and alanine (PDB code [[5j8q]])' scene=''> |
== Function == | == Function == | ||
'''Cysteine desulfurase''' (SUFS) catalyzes the conversion of L-cysteine to L-alanine and sulfane sulfur. SUFS has a role in the biosynthesis of Fe-S custers, thiamine, thionucleosides, biotin, lipoic acid, molybdopterin and NAD<ref>PMID:12382038</ref>. SUFS is a PLP-dependent enzyme. | '''Cysteine desulfurase''' (SUFS) catalyzes the conversion of L-cysteine to L-alanine and sulfane sulfur. SUFS has a role in the biosynthesis of Fe-S custers, thiamine, thionucleosides, biotin, lipoic acid, molybdopterin and NAD<ref>PMID:12382038</ref>. SUFS is a PLP-dependent enzyme. | ||
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| - | == Disease == | ||
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| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
| - | The structure | + | The structure of SUFS containing the cofactor PLP bound to Lys224. Cys361 is the nucleophilic catalytic residue. The reaction product alanine is bound near the Cys361-persulfide<ref>PMID:27382962</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 11:22, 5 November 2018
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3D structures of cysteine desulfurase
Updated on 05-November-2018
References
- ↑ 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
