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5w7k

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Current revision (14:14, 13 March 2024) (edit) (undo)
 
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<StructureSection load='5w7k' size='340' side='right'caption='[[5w7k]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='5w7k' size='340' side='right'caption='[[5w7k]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5w7k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_219.30 Cbs 219.30]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W7K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5w7k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_oxalicum Penicillium oxalicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W7K FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.994&#8491;</td></tr>
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<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=5w7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w7k OCA], [http://pdbe.org/5w7k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w7k RCSB], [http://www.ebi.ac.uk/pdbsum/5w7k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w7k ProSAT]</span></td></tr>
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<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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5w7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w7k OCA], [https://pdbe.org/5w7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w7k RCSB], [https://www.ebi.ac.uk/pdbsum/5w7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w7k ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1B2TT18_PENOX A0A1B2TT18_PENOX]
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Antimicrobial and anti-proliferative meleagrin and oxaline are roquefortine C-derived alkaloids produced by fungi of the genus Penicillium. Tandem O-methylations complete the biosynthesis of oxaline from glandicoline B through meleagrin. Currently, little is known about the role of these methylation patterns in the bioactivity profile of meleagrin and oxaline. To establish the structural and mechanistic basis of methylation in these pathways, crystal structures were determined for two late-stage methyltransferases in the oxaline and meleagrin gene clusters from Penicillium oxalicum and Penicillium chrysogenum. The homologous enzymes OxaG and RoqN were shown to catalyze penultimate hydroxylamine O-methylation to generate meleagrin in vitro. Crystal structures of these enzymes in the presence of methyl donor S-adenosylmethionine revealed an open active site, which lacks an apparent base indicating that catalysis is driven by proximity effects. OxaC was shown to methylate meleagrin to form oxaline in vitro, the terminal pathway product. Crystal structures of OxaC in a pseudo-Michaelis complex containing sinefungin and meleagrin, and in a product complex containing S-adenosyl-homocysteine and oxaline, reveal key active site residues with His313 serving as a base that is activated by Glu369. These data provide structural insights into the enzymatic methylation of these alkaloids that include a rare hydroxylamine oxygen acceptor, and can be used to guide future efforts towards selective derivatization and structural diversification and establishing the role of methylation in bioactivity.
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Unveiling sequential late-stage methyltransferase reactions in the meleagrin/oxaline biosynthetic pathway.,Newmister SA, Romminger S, Schmidt JJ, Williams RM, Smith JL, Berlinck RGS, Sherman DH Org Biomol Chem. 2018 Aug 24. doi: 10.1039/c8ob01565a. PMID:30141817<ref>PMID:30141817</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5w7k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cbs 219 30]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Berlinck, R G.S]]
 
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[[Category: Newmister, S A]]
 
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[[Category: Romminger, S]]
 
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[[Category: Schmidt, J J]]
 
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[[Category: Sherman, D H]]
 
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[[Category: Smith, J L]]
 
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[[Category: Williams, R M]]
 
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[[Category: Indole alkaloid]]
 
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[[Category: Methyltransferase]]
 
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[[Category: Oxaline]]
 
[[Category: Penicillium oxalicum]]
[[Category: Penicillium oxalicum]]
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[[Category: Transferase]]
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[[Category: Berlinck RGS]]
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[[Category: Newmister SA]]
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[[Category: Romminger S]]
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[[Category: Schmidt JJ]]
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[[Category: Sherman DH]]
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[[Category: Smith JL]]
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[[Category: Williams RM]]

Current revision

Crystal structure of OxaG

PDB ID 5w7k

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