8f7h

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'''Unreleased structure'''
 
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The entry 8f7h is ON HOLD until Paper Publication
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==The condensation domain of surfactin A synthetase C variant 18b in space group P212121==
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<StructureSection load='8f7h' size='340' side='right'caption='[[8f7h]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8f7h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F7H FirstGlance]. <br>
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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]] 1.93&#8491;</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=GOL:GLYCEROL'>GOL</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=8f7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f7h OCA], [https://pdbe.org/8f7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f7h RCSB], [https://www.ebi.ac.uk/pdbsum/8f7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f7h ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Engineered biosynthetic assembly lines could revolutionize the sustainable production of bioactive natural product analogs. Although yeast display is a proven, powerful tool for altering the substrate specificity of gatekeeper adenylation domains in nonribosomal peptide synthetases (NRPSs), comparable strategies for other components of these megaenzymes have not been described. Here we report a high-throughput approach for engineering condensation (C) domains responsible for peptide elongation. We show that a 120-kDa NRPS module, displayed in functional form on yeast, can productively interact with an upstream module, provided in solution, to produce amide products tethered to the yeast surface. Using this system to screen a large C-domain library, we reprogrammed a surfactin synthetase module to accept a fatty acid donor, increasing catalytic efficiency for this noncanonical substrate &gt;40-fold. Because C domains can function as selectivity filters in NRPSs, this methodology should facilitate the precision engineering of these molecular assembly lines.
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Authors:
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High-throughput reprogramming of an NRPS condensation domain.,Folger IB, Frota NF, Pistofidis A, Niquille DL, Hansen DA, Schmeing TM, Hilvert D Nat Chem Biol. 2024 Jun;20(6):761-769. doi: 10.1038/s41589-023-01532-x. Epub 2024 , Feb 2. PMID:38308044<ref>PMID:38308044</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8f7h" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus subtilis]]
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[[Category: Large Structures]]
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[[Category: Folger IB]]
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[[Category: Frota NF]]
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[[Category: Hilvert D]]
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[[Category: Pistofidis A]]
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[[Category: Schmeing M]]

Current revision

The condensation domain of surfactin A synthetase C variant 18b in space group P212121

PDB ID 8f7h

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