6p29

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Current revision (14:53, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6p29' size='340' side='right'caption='[[6p29]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6p29' size='340' side='right'caption='[[6p29]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6p29]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"alteromonas_luteo-violaceus"_(sic)_gauthier_1976 "alteromonas luteo-violaceus" (sic) gauthier 1976]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P29 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6p29]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_luteoviolacea Pseudoalteromonas luteoviolacea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P29 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=NQ7:(5S)-2-amino-5-[(1R)-1-(1H-indol-3-yl)ethyl]-1,3-oxazol-4(5H)-one'>NQ7</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N473_05385 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43657 "Alteromonas luteo-violaceus" (sic) Gauthier 1976])</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=NQ7:(5S)-2-amino-5-[(1R)-1-(1H-indol-3-yl)ethyl]-1,3-oxazol-4(5H)-one'>NQ7</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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=6p29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p29 OCA], [http://pdbe.org/6p29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p29 RCSB], [http://www.ebi.ac.uk/pdbsum/6p29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p29 ProSAT]</span></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=6p29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p29 OCA], [https://pdbe.org/6p29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p29 RCSB], [https://www.ebi.ac.uk/pdbsum/6p29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p29 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/A0A167HII1_9GAMM A0A167HII1_9GAMM]
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Microbes produce specialized metabolites to thrive in their natural habitats. However, it is rare that a given specialized metabolite is biosynthesized via pathways with distinct intermediates and enzymes. Here, we show that the core assembly mechanism of the antibiotic indolmycin in marine gram-negative Pseudoalteromonas luteoviolacea is distinct from its counterpart in terrestrial gram-positive Streptomyces species, with a molecule that is a shunt product in the Streptomyces pathway employed as a biosynthetic substrate for a novel metal-independent N-demethylindolmycin synthase in the P. luteoviolacea pathway. To provide insight into this reaction, we solved the 1.5 A resolution structure in complex with product and identified the active site residues. Guided by our biosynthetic insights, we then engineered the Streptomyces indolmycin producer for titer improvement. This study provides a paradigm for understanding how two unique routes to a microbial specialized metabolite can emerge from convergent biosynthetic transformations.
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Convergent biosynthetic transformations to a bacterial specialized metabolite.,Du YL, Higgins MA, Zhao G, Ryan KS Nat Chem Biol. 2019 Aug 12. pii: 10.1038/s41589-019-0331-5. doi:, 10.1038/s41589-019-0331-5. PMID:31406372<ref>PMID:31406372</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 6p29" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Du, Y L]]
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[[Category: Pseudoalteromonas luteoviolacea]]
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[[Category: Higgins, M A]]
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[[Category: Du YL]]
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[[Category: Ryan, K S]]
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[[Category: Higgins MA]]
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[[Category: Zhao, G]]
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[[Category: Ryan KS]]
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[[Category: Biosynthetic protein]]
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[[Category: Zhao G]]
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[[Category: N-demethylindolmycin synthase]]
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Current revision

N-demethylindolmycin synthase (PluN2) in complex with N-demethylindolmycin

PDB ID 6p29

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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