7pg7
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7pg7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_tsukubensis Streptomyces tsukubensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PG7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pg7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_tsukubensis Streptomyces tsukubensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PG7 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 1.51Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=7pg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pg7 OCA], [https://pdbe.org/7pg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pg7 RCSB], [https://www.ebi.ac.uk/pdbsum/7pg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pg7 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=7pg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pg7 OCA], [https://pdbe.org/7pg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pg7 RCSB], [https://www.ebi.ac.uk/pdbsum/7pg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pg7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/I2N5E8_STRT9 I2N5E8_STRT9] | [https://www.uniprot.org/uniprot/I2N5E8_STRT9 I2N5E8_STRT9] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Streptomyces soil bacteria produce hundreds of anthracycline anticancer agents with a relatively conserved set of genes. This diversity depends on the rapid evolution of biosynthetic enzymes to acquire novel functionalities. Previous work has identified S-adenosyl-l-methionine-dependent methyltransferase-like proteins that catalyze 4-O-methylation, 10-decarboxylation, or 10-hydroxylation, with additional differences in substrate specificities. Here we focused on four protein regions to generate chimeric enzymes using sequences from four distinct subfamilies to elucidate their influence in catalysis. Combined with structural studies we managed to depict factors that influence gain-of-hydroxylation, loss-of-methylation, and substrate selection. The engineering expanded the catalytic repertoire to include novel 9,10-elimination activity, and 4-O-methylation and 10-decarboxylation of unnatural substrates. The work provides an instructive account on how the rise of diversity of microbial natural products may occur through subtle changes in biosynthetic enzymes. | ||
| - | |||
| - | Evolution-inspired engineering of anthracycline methyltransferases.,Dinis P, Tirkkonen H, Wandi BN, Siitonen V, Niemi J, Grocholski T, Metsa-Ketela M PNAS Nexus. 2023 Feb 28;2(2):pgad009. doi: 10.1093/pnasnexus/pgad009. eCollection , 2023 Feb. PMID:36874276<ref>PMID:36874276</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7pg7" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
10-decarboxylase TamK from Streptomyces tsukubaensis
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