8f7i: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8f7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f7i OCA], [https://pdbe.org/8f7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f7i RCSB], [https://www.ebi.ac.uk/pdbsum/8f7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f7i ProSAT]</span></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=8f7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f7i OCA], [https://pdbe.org/8f7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f7i RCSB], [https://www.ebi.ac.uk/pdbsum/8f7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f7i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | |||
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 >40-fold. Because C domains can function as selectivity filters in NRPSs, this methodology should facilitate the precision engineering of these molecular assembly lines. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 8f7i" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 05:24, 12 June 2024
The condensation domain of surfactin A synthetase C variant 18b in space group P43212
| ||||||||||||
