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| | <StructureSection load='6tho' size='340' side='right'caption='[[6tho]], [[Resolution|resolution]] 1.09Å' scene=''> | | <StructureSection load='6tho' size='340' side='right'caption='[[6tho]], [[Resolution|resolution]] 1.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tho]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6THO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6THO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tho]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6THO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6THO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</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]] 1.09Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr0975, alr0975 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></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=6tho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tho OCA], [https://pdbe.org/6tho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tho RCSB], [https://www.ebi.ac.uk/pdbsum/6tho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tho ProSAT]</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=6tho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tho OCA], [https://pdbe.org/6tho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tho RCSB], [https://www.ebi.ac.uk/pdbsum/6tho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tho ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8YY76_NOSS1 Q8YY76_NOSS1] |
| | <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: Anabaena 7120]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blankenfeldt, W]] | + | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] |
| - | [[Category: Feiler, C G]] | + | [[Category: Blankenfeldt W]] |
| - | [[Category: Chelating heavy atom]] | + | [[Category: Feiler CG]] |
| - | [[Category: Detoxification]]
| + | |
| - | [[Category: Glutathione]]
| + | |
| - | [[Category: Phytochelatin]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q8YY76_NOSS1
Publication Abstract from PubMed
Phytochelatins (PCs) are nonribosomal thiol-rich oligopeptides synthetized from glutathione (GSH) in a gamma-glutamylcysteinyl transpeptidation reaction catalyzed by PC synthases (PCSs). Ubiquitous in plant and present in some invertebrates, PCSs are involved in metal detoxification and homeostasis. The PCS-like enzyme from the cyanobacterium Nostoc sp. (NsPCS) is considered to be an evolutionary precursor enzyme of genuine PCSs because it shows sufficient sequence similarity for homology to the catalytic domain of the eukaryotic PCSs and shares the peptidase activity consisting in the deglycination of GSH. In this work, we investigate the catalytic mechanism of NsPCS by combining structural, spectroscopic, thermodynamic, and theoretical techniques. We report several crystal structures of NsPCS capturing different states of the catalyzed chemical reaction: (i) the structure of the wild-type enzyme (wt-NsPCS); (ii) the high-resolution structure of the gamma-glutamyl-cysteine acyl-enzyme intermediate (acyl-NsPCS); and (iii) the structure of an inactive variant of NsPCS, with the catalytic cysteine mutated into serine (C70S-NsPCS). We characterize NsPCS as a relatively slow enzyme whose activity is sensitive to the redox state of the substrate. Namely, NsPCS is active with reduced glutathione (GSH), but is inhibited by oxidized glutathione (GSSG) because the cleavage product is not released from the enzyme. Our biophysical analysis led us to suggest that the biological function of NsPCS is being a part of a redox sensing system. In addition, we propose a mechanism how PCS-like enzymes may have evolved toward genuine PCS enzymes.
Structural and Biophysical Analysis of the Phytochelatin-Synthase-Like Enzyme from Nostoc sp. Shows That Its Protease Activity is Sensitive to the Redox State of the Substrate.,Gisdon FJ, Feiler CG, Kempf O, Foerster JM, Haiss J, Blankenfeldt W, Ullmann GM, Bombarda E ACS Chem Biol. 2022 Apr 15;17(4):883-897. doi: 10.1021/acschembio.1c00941. Epub, 2022 Apr 4. PMID:35377603[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gisdon FJ, Feiler CG, Kempf O, Foerster JM, Haiss J, Blankenfeldt W, Ullmann GM, Bombarda E. Structural and Biophysical Analysis of the Phytochelatin-Synthase-Like Enzyme from Nostoc sp. Shows That Its Protease Activity is Sensitive to the Redox State of the Substrate. ACS Chem Biol. 2022 Apr 15;17(4):883-897. doi: 10.1021/acschembio.1c00941. Epub, 2022 Apr 4. PMID:35377603 doi:http://dx.doi.org/10.1021/acschembio.1c00941
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