Sulfurtransferase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='340' side='right' caption='Human mercaptopyruvate sulfurtransferase with mercaptocysteine complex with pyruvate, sulfate (PDB entry [[4jgt]])' scene='46/468089/Cv/2'> |
== Function == | == Function == | ||
'''Sulfurtransferase''' (ST) are enzymes which transfer sulfur-containing groups<ref>PMID:20135153</ref>. | '''Sulfurtransferase''' (ST) are enzymes which transfer sulfur-containing groups<ref>PMID:20135153</ref>. | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The <scene name='46/468089/Cv/ | + | The <scene name='46/468089/Cv/5'>active site of MST contains mercaptocysteine and pyruvate</scene><ref>PMID:23698001</ref>. Water molecules are shown as red spheres. |
</StructureSection> | </StructureSection> | ||
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*Sulfurtransferase | *Sulfurtransferase | ||
| + | **[[1boh]], [[1boi]], [[1orb]], [[1rhd]], [[1rhs]] – bST – bovine<br /> | ||
| + | **[[1dp2]] – bST + lipoate<br /> | ||
**[[3lvj]], [[3lvk]] – EcST TusA + cysteine desulfurase - ''Escherichia coli''<br /> | **[[3lvj]], [[3lvk]] – EcST TusA + cysteine desulfurase - ''Escherichia coli''<br /> | ||
**[[2fsx]] – MtST – ''Mycobacterium tuberculosis''<br /> | **[[2fsx]] – MtST – ''Mycobacterium tuberculosis''<br /> | ||
**[[1uar]] – ST – ''Thermus thermophilus''<br /> | **[[1uar]] – ST – ''Thermus thermophilus''<br /> | ||
| - | **[[ | + | **[[6ktx]], [[6h99]] – ClST – ''Chlorobium limicola''<br /> |
| - | **[[ | + | **[[6ku1]], [[6ku2]], [[6kw0]] – ClST (mutant) + ergothioneine<br /> |
| + | **[[6h9a]], [[6ktv]], [[6ktw]] – ClST + hercynine<br /> | ||
| + | **[[6kvz]], [[6kvy]], [[6kvw]], [[6ktz]] – ClST (mutant) + hercynine<br /> | ||
| + | **[[7syb]] – ST – ''Acinetobacter baumanni''<br /> | ||
*Mercaptopyruvate sulfurtransferase | *Mercaptopyruvate sulfurtransferase | ||
| + | **[[3olh]], [[4jgt]] – MST - human<br /> | ||
| + | **[[5wqj]], [[5wqk]] – MST (mutant) + inhibitor – mouse<br /> | ||
**[[1okg]] – MST (mutant) – ''Leishmania major'' | **[[1okg]] – MST (mutant) – ''Leishmania major'' | ||
**[[1urh]] – EcMST | **[[1urh]] – EcMST | ||
| - | **[[3olh]], [[4jgt]] – MST - human<br /> | ||
**[[5wqj]], [[5wqk]] – MST + inhibitor - mouse<br /> | **[[5wqj]], [[5wqk]] – MST + inhibitor - mouse<br /> | ||
| - | *Thiosulfate sulfurtransferase | + | *Thiosulfate sulfurtransferase or rhodanese |
| + | **[[6bev]] – hTST D1<br /> | ||
| + | **[[2ora]], [[8q5z]] – bTST<br /> | ||
| + | **[[3utn]] – yTST Tum1 – yeast<br /> | ||
| + | **[[6k6r]] – yTST Rdl2<br /> | ||
**[[1yt8]] – TST – ''Pseudomonas aeruginosa''<br /> | **[[1yt8]] – TST – ''Pseudomonas aeruginosa''<br /> | ||
**[[3hwi]], [[3p3a]] – MtTST<br /> | **[[3hwi]], [[3p3a]] – MtTST<br /> | ||
**[[3hzu]] – MtTST Ssea<br /> | **[[3hzu]] – MtTST Ssea<br /> | ||
| - | **[[2ora]] – bTST<br /> | ||
| - | **[[3utn]] – TST Tum1 – yeast<br /> | ||
**[[1e0c]] – AvST – ''Azotobacter vinelandii''<br /> | **[[1e0c]] – AvST – ''Azotobacter vinelandii''<br /> | ||
**[[1gmx]], [[1gn0]] – EcST Glpe<br /> | **[[1gmx]], [[1gn0]] – EcST Glpe<br /> | ||
| - | **[[1h4k]] – | + | *Zinc-dependent sulfurtransferase SufU |
| + | |||
| + | **[[6jzv]], [[6jzw]] – BsZST + Zn – ''Bacillus subtilis''<br /> | ||
| + | **[[5xt5]] – BsZST + Zn + PLP <br /> | ||
| + | **[[5xt6]] – BsZST + cysteine desulferase + Zn + PLP derivative<br /> | ||
| + | |||
| + | **[[1h4k]] – AvZST + hypophosphite | ||
| - | **[[1h4m]] – | + | **[[1h4m]] – AvZST + phosphate |
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D Structures of sulfurtransferase
Updated on 01-March-2024
References
- ↑ Papenbrock J, Guretzki S, Henne M. Latest news about the sulfurtransferase protein family of higher plants. Amino Acids. 2011 Jun;41(1):43-57. doi: 10.1007/s00726-010-0478-6. Epub 2010 Feb , 5. PMID:20135153 doi:http://dx.doi.org/10.1007/s00726-010-0478-6
- ↑ Morton NM, Beltram J, Carter RN, Michailidou Z, Gorjanc G, McFadden C, Barrios-Llerena ME, Rodriguez-Cuenca S, Gibbins MT, Aird RE, Moreno-Navarrete JM, Munger SC, Svenson KL, Gastaldello A, Ramage L, Naredo G, Zeyda M, Wang ZV, Howie AF, Saari A, Sipila P, Stulnig TM, Gudnason V, Kenyon CJ, Seckl JR, Walker BR, Webster SP, Dunbar DR, Churchill GA, Vidal-Puig A, Fernandez-Real JM, Emilsson V, Horvat S. Genetic identification of thiosulfate sulfurtransferase as an adipocyte-expressed antidiabetic target in mice selected for leanness. Nat Med. 2016 Jul;22(7):771-9. doi: 10.1038/nm.4115. Epub 2016 Jun 6. PMID:27270587 doi:http://dx.doi.org/10.1038/nm.4115
- ↑ Nakamura T, Yamaguchi Y, Sano H. Plant mercaptopyruvate sulfurtransferases: molecular cloning, subcellular localization and enzymatic activities. Eur J Biochem. 2000 Sep;267(17):5621-30. PMID:10951223
- ↑ Shatalin K, Shatalina E, Mironov A, Nudler E. H2S: a universal defense against antibiotics in bacteria. Science. 2011 Nov 18;334(6058):986-90. doi: 10.1126/science.1209855. PMID:22096201 doi:http://dx.doi.org/10.1126/science.1209855
- ↑ Yadav PK, Yamada K, Chiku T, Koutmos M, Banerjee R. Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase. J Biol Chem. 2013 May 22. PMID:23698001 doi:10.1074/jbc.M113.466177
