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| | <StructureSection load='6a6g' size='340' side='right'caption='[[6a6g]], [[Resolution|resolution]] 2.49Å' scene=''> | | <StructureSection load='6a6g' size='340' side='right'caption='[[6a6g]], [[Resolution|resolution]] 2.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6a6g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49647 Atcc 49647]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A6G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6A6G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6a6g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fervidobacterium_islandicum Fervidobacterium islandicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A6G FirstGlance]. <br> |
| - | </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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NA23_08315 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2423 ATCC 49647]), NA23_08310 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2423 ATCC 49647])</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=6a6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a6g OCA], [https://pdbe.org/6a6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a6g RCSB], [https://www.ebi.ac.uk/pdbsum/6a6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a6g ProSAT]</span></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://proteopedia.org/fgij/fg.htm?mol=6a6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a6g OCA], [http://pdbe.org/6a6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a6g RCSB], [http://www.ebi.ac.uk/pdbsum/6a6g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a6g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A1B0VPZ3_FERIS A0A1B0VPZ3_FERIS]] Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.[RuleBase:RU004506] | + | [https://www.uniprot.org/uniprot/A0A1B0VPZ3_FERIS A0A1B0VPZ3_FERIS] Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.[RuleBase:RU004506] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 49647]] | + | [[Category: Fervidobacterium islandicum]] |
| - | [[Category: Cysteine desulfurase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dhanasingh, I]] | + | [[Category: Dhanasingh I]] |
| - | [[Category: Jin, H S]] | + | [[Category: Jin HS]] |
| - | [[Category: Lee, D W]] | + | [[Category: Lee DW]] |
| - | [[Category: Lee, S H]] | + | [[Category: Lee SH]] |
| - | [[Category: Suf gene cluster]]
| + | |
| - | [[Category: Thermophile]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
6a6g is a 4 chain structure with sequence from Fervidobacterium islandicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.49Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A0A1B0VPZ3_FERIS Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.[RuleBase:RU004506]
Publication Abstract from PubMed
Most extremophilic anaerobes possess a sulfur formation (Suf) system for Fe-S cluster biogenesis. In addition to its essential role in redox chemistry and stress responses of Fe-S cluster proteins, the Suf system may play an important role in keratin degradation by Fervidobacterium islandicum AW-1. Comparative genomics of the order Thermotogales revealed that the feather-degrading F. islandicum AW-1 has a complete Suf-like machinery (SufCBDSU) that is highly expressed in cells grown on native feathers in the absence of elemental sulfur (S(0) ). On the other hand, F. islandicum AW-1 exhibited a significant retardation in the Suf system-mediated keratin degradation in the presence of S(0) . Detailed differential expression analysis of sulfur assimilation machineries unveiled the mechanism by which an efficient sulfur delivery from persulfurated SufS to SufU is achieved during keratinolysis under sulfur starvation. Indeed, addition of SufS-SufU to cell extracts containing keratinolytic proteases accelerated keratin decomposition in vitro under reducing conditions. Remarkably, mass spectrometric analysis of extracellular and intracellular levels of amino acids suggested that redox homeostasis within cells coupled to extracellular cysteine and cystine recycling might be a prerequisite for keratinolysis. Taken together, these results suggest that the Suf-like machinery including the SufS-SufU complex may contribute to sulfur availability for an extracellular reducing environment as well as intracellular redox homeostasis through cysteine released from keratin hydrolysate under starvation conditions.
The sulfur formation system mediating extracellular cysteine-cystine recycling in Fervidobacterium islandicum AW-1 is associated with keratin degradation.,Jin HS, Dhanasingh I, Sung JY, La JW, Lee Y, Lee EM, Kang Y, Lee DY, Lee SH, Lee DW Microb Biotechnol. 2020 Dec 15. doi: 10.1111/1751-7915.13717. PMID:33320434[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jin HS, Dhanasingh I, Sung JY, La JW, Lee Y, Lee EM, Kang Y, Lee DY, Lee SH, Lee DW. The sulfur formation system mediating extracellular cysteine-cystine recycling in Fervidobacterium islandicum AW-1 is associated with keratin degradation. Microb Biotechnol. 2020 Dec 15. doi: 10.1111/1751-7915.13717. PMID:33320434 doi:http://dx.doi.org/10.1111/1751-7915.13717
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