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| | <StructureSection load='6dg3' size='340' side='right'caption='[[6dg3]], [[Resolution|resolution]] 2.94Å' scene=''> | | <StructureSection load='6dg3' size='340' side='right'caption='[[6dg3]], [[Resolution|resolution]] 2.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6dg3]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacpl Lacpl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DG3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dg3]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactiplantibacillus_plantarum_WCFS1 Lactiplantibacillus plantarum WCFS1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DG3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.944Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">larE, lp_0109 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220668 LACPL])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6dg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dg3 OCA], [http://pdbe.org/6dg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dg3 RCSB], [http://www.ebi.ac.uk/pdbsum/6dg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dg3 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=6dg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dg3 OCA], [https://pdbe.org/6dg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dg3 RCSB], [https://www.ebi.ac.uk/pdbsum/6dg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dg3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LARE_LACPL LARE_LACPL]] Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Catalyzes the ATP-dependent incorporation of two sulfur atoms in pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN) to yield pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN). The source of sulfur is the enzyme itself: Cys-176 of LarE is the sulfur donor, thereby being converted into dehydroalanine, and is not regenerated in vivo. Thus, two molecules of LarE undergo sacrificial sulfur transfer to create one P2TMN (PubMed:27114550). Binds nickel (PubMed:24710389). Is required for the activation of the lactate racemase LarA (PubMed:24710389). May also be involved in the activation of other nickel-pincer cofactor-dependent enzymes (PubMed:27114550).<ref>PMID:24710389</ref> <ref>PMID:27114550</ref> | + | [https://www.uniprot.org/uniprot/LARE_LACPL LARE_LACPL] Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Catalyzes the ATP-dependent incorporation of two sulfur atoms in pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN) to yield pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN). The source of sulfur is the enzyme itself: Cys-176 of LarE is the sulfur donor, thereby being converted into dehydroalanine, and is not regenerated in vivo. Thus, two molecules of LarE undergo sacrificial sulfur transfer to create one P2TMN (PubMed:27114550). Binds nickel (PubMed:24710389). Is required for the activation of the lactate racemase LarA (PubMed:24710389). May also be involved in the activation of other nickel-pincer cofactor-dependent enzymes (PubMed:27114550).<ref>PMID:24710389</ref> <ref>PMID:27114550</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lacpl]] | + | [[Category: Lactiplantibacillus plantarum WCFS1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fellner, M]] | + | [[Category: Fellner M]] |
| - | [[Category: Hausinger, R P]] | + | [[Category: Hausinger RP]] |
| - | [[Category: Hu, J]] | + | [[Category: Hu J]] |
| - | [[Category: Ampylation]]
| + | |
| - | [[Category: Atp pyrophophatase domain]]
| + | |
| - | [[Category: Caesium]]
| + | |
| - | [[Category: Hexamer]]
| + | |
| - | [[Category: Lactate]]
| + | |
| - | [[Category: Lactate racemase]]
| + | |
| - | [[Category: Lactate racemization]]
| + | |
| - | [[Category: Lar]]
| + | |
| - | [[Category: Lare]]
| + | |
| - | [[Category: Pp-loop]]
| + | |
| - | [[Category: Sulfur transferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Trimer]]
| + | |
| Structural highlights
Function
LARE_LACPL Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Catalyzes the ATP-dependent incorporation of two sulfur atoms in pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN) to yield pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN). The source of sulfur is the enzyme itself: Cys-176 of LarE is the sulfur donor, thereby being converted into dehydroalanine, and is not regenerated in vivo. Thus, two molecules of LarE undergo sacrificial sulfur transfer to create one P2TMN (PubMed:27114550). Binds nickel (PubMed:24710389). Is required for the activation of the lactate racemase LarA (PubMed:24710389). May also be involved in the activation of other nickel-pincer cofactor-dependent enzymes (PubMed:27114550).[1] [2]
References
- ↑ Desguin B, Goffin P, Viaene E, Kleerebezem M, Martin-Diaconescu V, Maroney MJ, Declercq JP, Soumillion P, Hols P. Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system. Nat Commun. 2014 Apr 7;5:3615. doi: 10.1038/ncomms4615. PMID:24710389 doi:http://dx.doi.org/10.1038/ncomms4615
- ↑ Desguin B, Soumillion P, Hols P, Hausinger RP. Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion. Proc Natl Acad Sci U S A. 2016 May 17;113(20):5598-603. doi:, 10.1073/pnas.1600486113. Epub 2016 Apr 25. PMID:27114550 doi:http://dx.doi.org/10.1073/pnas.1600486113
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