View source for 8rdn


==Holomycin methyltransferase DtpM with SAH and XRD-271==
<StructureSection load='8rdn' size='340' side='right'caption='[[8rdn]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8rdn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenorhabdus_doucetiae_FRM16_=_DSM_17909 Xenorhabdus doucetiae FRM16 = DSM 17909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RDN 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=YRH:~{N}-(5-oxidanylidene-4~{H}-[1,2]dithiolo[4,3-b]pyrrol-6-yl)hexanamide'>YRH</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=8rdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rdn OCA], [https://pdbe.org/8rdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rdn RCSB], [https://www.ebi.ac.uk/pdbsum/8rdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rdn ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Dithiolopyrrolone (DTP) natural products are produced by several different bacteria and have potent antibacterial, antifungal and anticancer activities. While the amide of their DTP core can be methylated to fine-tune bioactivity, the enzyme responsible for the amide N-methylation has remained elusive in most taxa. Here, we identified the amide methyltransferase XrdM that is responsible for xenorhabdin (XRD) methylation in Xenorhabdus doucetiae but encoded outside of the XRD gene cluster. XrdM turned out to be isofunctional with the recently reported methyltransferase DtpM, that is involved in the biosynthesis of the DTP thiolutin, although its X-ray structure is unrelated to that of DtpM. To investigate the structural basis for ligand binding in both enzymes, we used X-ray crystallography, modeling, site-directed mutagenesis, and kinetic activity assays. Our study expands the limited knowledge of post-non-ribosomal peptide synthetase (NRPS) amide methylation in DTP biosynthesis and reveals an example of convergent evolution of two structurally completely different enzymes for the same reaction in different organisms.

Isofunctional but Structurally Different Methyltransferases for Dithiolopyrrolone Diversification.,Su L, Huber EM, Westphalen M, Gellner J, Bode E, Kobel T, Grun P, Alanjary MM, Glatter T, Cirnski K, Muller R, Schindler D, Groll M, Bode HB Angew Chem Int Ed Engl. 2024 Aug 26:e202410799. doi: 10.1002/anie.202410799. PMID:39185606<ref>PMID:39185606</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8rdn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Xenorhabdus doucetiae FRM16 = DSM 17909]]
[[Category: Groll M]]
[[Category: Huber EM]]