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| | <StructureSection load='6u1r' size='340' side='right'caption='[[6u1r]], [[Resolution|resolution]] 1.79Å' scene=''> | | <StructureSection load='6u1r' size='340' side='right'caption='[[6u1r]], [[Resolution|resolution]] 1.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6u1r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_wollei Lyngbya wollei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U1R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U1R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6u1r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Microseira_wollei Microseira wollei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U1R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.792Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sxtG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=467598 Lyngbya wollei])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=6u1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u1r OCA], [http://pdbe.org/6u1r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u1r RCSB], [http://www.ebi.ac.uk/pdbsum/6u1r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u1r 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=6u1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u1r OCA], [https://pdbe.org/6u1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u1r RCSB], [https://www.ebi.ac.uk/pdbsum/6u1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u1r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C3RVP0_9CYAN C3RVP0_9CYAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lyngbya wollei]] | + | [[Category: Microseira wollei]] |
| - | [[Category: Koutmos, M]] | + | [[Category: Koutmos M]] |
| - | [[Category: Lukowski, A L]] | + | [[Category: Lukowski AL]] |
| - | [[Category: Mallik, L]] | + | [[Category: Mallik L]] |
| - | [[Category: Narayan, A R.H]] | + | [[Category: Narayan ARH]] |
| - | [[Category: Amidinotransferase]]
| + | |
| - | [[Category: Saxitoxin biosynthetic pathway]]
| + | |
| - | [[Category: Sxtg]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
C3RVP0_9CYAN
Publication Abstract from PubMed
Secondary metabolites are assembled by enzymes that often perform reactions with high selectivity and specificity. Many of these enzymes also tolerate variations in substrate structure, exhibiting promiscuity that enables various applications of a given biocatalyst. However, initial enzyme characterization studies frequently do not explore beyond the native substrates. This limited assessment of substrate scope contributes to the difficulty of identifying appropriate enzymes for specific synthetic applications. Here, we report the natural function of cyanobacterial SxtG, an amidinotransferase involved in the biosynthesis of paralytic shellfish toxins, and demonstrate its ability to modify a breadth of non-native substrates. In addition, we report the first X-ray crystal structure of SxtG, which provides rationale for this enzyme's substrate scope. Taken together, these data confirm the function of SxtG and exemplify its potential utility in biocatalytic synthesis.
Substrate Promiscuity of a Paralytic Shellfish Toxin Amidinotransferase.,Lukowski AL, Mallik L, Hinze ME, Carlson BM, Ellinwood DC, Pyser JB, Koutmos M, Narayan ARH ACS Chem Biol. 2020 Feb 14. doi: 10.1021/acschembio.9b00964. PMID:32058687[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lukowski AL, Mallik L, Hinze ME, Carlson BM, Ellinwood DC, Pyser JB, Koutmos M, Narayan ARH. Substrate Promiscuity of a Paralytic Shellfish Toxin Amidinotransferase. ACS Chem Biol. 2020 Feb 14. doi: 10.1021/acschembio.9b00964. PMID:32058687 doi:http://dx.doi.org/10.1021/acschembio.9b00964
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