7fe5: Difference between revisions
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==AvmM Catalyzes Macrocyclization in Alchivemycin A Biosynthesis== | |||
<StructureSection load='7fe5' size='340' side='right'caption='[[7fe5]], [[Resolution|resolution]] 2.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7fe5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._NBRC_109436 Streptomyces sp. NBRC 109436]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FE5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=7fe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fe5 OCA], [https://pdbe.org/7fe5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fe5 RCSB], [https://www.ebi.ac.uk/pdbsum/7fe5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fe5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A8F7LEJ5_9ACTN A0A8F7LEJ5_9ACTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Macrocyclization is an important process that affords morphed scaffold in biosynthesis of bioactive natural products. Nature has adapted diverse biosynthetic strategies to form macrocycles. In this work, we report the identification and characterization of a small enzyme AvmM that can catalyze the construction of a 16-membered macrocyclic ring in the biosynthesis of alchivemycin A (1). We show through in vivo gene deletion, in vitro biochemical assay and isotope labelling experiments that AvmM catalyzes tandem dehydration and Michael-type addition to generate the core scaffold of 1. Mechanistic studies by crystallography, DFT calculations and MD simulations of AvmM reveal that the reactions are achieved with assistance from the special tenuazonic acid like moiety of substrate. Our results thus uncover an uncharacterized macrocyclization strategy in natural product biosynthesis. | |||
AvmM catalyses macrocyclization through dehydration/Michael-type addition in alchivemycin A biosynthesis.,Zhu HJ, Zhang B, Wei W, Liu SH, Xiang L, Zhu J, Jiao RH, Igarashi Y, Bashiri G, Liang Y, Tan RX, Ge HM Nat Commun. 2022 Aug 3;13(1):4499. doi: 10.1038/s41467-022-32088-4. PMID:35922406<ref>PMID:35922406</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7fe5" style="background-color:#fffaf0;"></div> | ||
[[Category: Ge | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces sp. NBRC 109436]] | |||
[[Category: Ge HM]] | |||
[[Category: Zhang B]] |
Latest revision as of 20:14, 29 November 2023
AvmM Catalyzes Macrocyclization in Alchivemycin A BiosynthesisAvmM Catalyzes Macrocyclization in Alchivemycin A Biosynthesis
Structural highlights
FunctionPublication Abstract from PubMedMacrocyclization is an important process that affords morphed scaffold in biosynthesis of bioactive natural products. Nature has adapted diverse biosynthetic strategies to form macrocycles. In this work, we report the identification and characterization of a small enzyme AvmM that can catalyze the construction of a 16-membered macrocyclic ring in the biosynthesis of alchivemycin A (1). We show through in vivo gene deletion, in vitro biochemical assay and isotope labelling experiments that AvmM catalyzes tandem dehydration and Michael-type addition to generate the core scaffold of 1. Mechanistic studies by crystallography, DFT calculations and MD simulations of AvmM reveal that the reactions are achieved with assistance from the special tenuazonic acid like moiety of substrate. Our results thus uncover an uncharacterized macrocyclization strategy in natural product biosynthesis. AvmM catalyses macrocyclization through dehydration/Michael-type addition in alchivemycin A biosynthesis.,Zhu HJ, Zhang B, Wei W, Liu SH, Xiang L, Zhu J, Jiao RH, Igarashi Y, Bashiri G, Liang Y, Tan RX, Ge HM Nat Commun. 2022 Aug 3;13(1):4499. doi: 10.1038/s41467-022-32088-4. PMID:35922406[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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