7tlp: Difference between revisions
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==Structure of Atopobium parvulum SufS K235R== | ==Structure of Atopobium parvulum SufS K235R== | ||
<StructureSection load='7tlp' size='340' side='right'caption='[[7tlp]]' scene=''> | <StructureSection load='7tlp' size='340' side='right'caption='[[7tlp]], [[Resolution|resolution]] 2.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TLP FirstGlance]. <br> | <table><tr><td colspan='2'>[[7tlp]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TLP FirstGlance]. <br> | ||
</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=7tlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tlp OCA], [https://pdbe.org/7tlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tlp RCSB], [https://www.ebi.ac.uk/pdbsum/7tlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tlp ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cysteine_desulfurase Cysteine desulfurase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7tlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tlp OCA], [https://pdbe.org/7tlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tlp RCSB], [https://www.ebi.ac.uk/pdbsum/7tlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tlp ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/C8W9P2_LANP1 C8W9P2_LANP1]] 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;"> | |||
== Publication Abstract from PubMed == | |||
Crohn's disease (CD) is characterized by the chronic inflammation of the gastrointestinal tract. A dysbiotic microbiome and a defective immune system are linked to CD, where hydrogen sulfide (H2 S) microbial producers positively correlate with the severity of the disease. Atopobium parvulum is a key H2 S producer from the microbiome of CD patients. In this study, the biochemical characterization of two Atopobium parvulum cysteine desulfurases, ApSufS and ApCsdB, shows that the enzymes are allosterically regulated. Structural analyses reveal that ApSufS forms a dimer with conserved characteristics observed in type II cysteine desulfurases. Four residues surrounding the active site are essential to catalyse cysteine desulfurylation, and a segment of short-chain residues grant access for substrate binding. A better understanding of ApSufS will help future avenues for CD treatment. | |||
Structural analysis of Atopobium parvulum SufS cysteine desulfurase linked to Crohn's disease.,Karunakaran G, Yang Y, Tremblay V, Ning Z, Martin J, Belaouad A, Figeys D, Brunzelle JS, Giguere PM, Stintzi A, Couture JF FEBS Lett. 2022 Feb 4. doi: 10.1002/1873-3468.14295. PMID:35122247<ref>PMID:35122247</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7tlp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cysteine desulfurase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Couture | [[Category: Couture, J F]] | ||
[[Category: Karunakaran G]] | [[Category: Karunakaran, G]] | ||
[[Category: Cysteine desulferase]] | |||
[[Category: Transferase]] | |||
Revision as of 14:55, 27 April 2022
Structure of Atopobium parvulum SufS K235RStructure of Atopobium parvulum SufS K235R
Structural highlights
Function[C8W9P2_LANP1] 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 PubMedCrohn's disease (CD) is characterized by the chronic inflammation of the gastrointestinal tract. A dysbiotic microbiome and a defective immune system are linked to CD, where hydrogen sulfide (H2 S) microbial producers positively correlate with the severity of the disease. Atopobium parvulum is a key H2 S producer from the microbiome of CD patients. In this study, the biochemical characterization of two Atopobium parvulum cysteine desulfurases, ApSufS and ApCsdB, shows that the enzymes are allosterically regulated. Structural analyses reveal that ApSufS forms a dimer with conserved characteristics observed in type II cysteine desulfurases. Four residues surrounding the active site are essential to catalyse cysteine desulfurylation, and a segment of short-chain residues grant access for substrate binding. A better understanding of ApSufS will help future avenues for CD treatment. Structural analysis of Atopobium parvulum SufS cysteine desulfurase linked to Crohn's disease.,Karunakaran G, Yang Y, Tremblay V, Ning Z, Martin J, Belaouad A, Figeys D, Brunzelle JS, Giguere PM, Stintzi A, Couture JF FEBS Lett. 2022 Feb 4. doi: 10.1002/1873-3468.14295. PMID:35122247[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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