View source for 8qnf


==Crystal structure of the Condensation domain TomBC from the Tomaymycin non-ribosomal peptide synthetase==
<StructureSection load='8qnf' size='340' side='right'caption='[[8qnf]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8qnf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_regensis Streptomyces regensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QNF 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=8qnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qnf OCA], [https://pdbe.org/8qnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qnf RCSB], [https://www.ebi.ac.uk/pdbsum/8qnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qnf ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the quest for new bioactive substances, nonribosomal peptide synthetases (NRPS) provide biodiversity by synthesizing nonproteinaceous peptides with high cellular activity. NRPS machinery consists of multiple modules, each catalyzing a unique series of chemical reactions. Incomplete understanding of the biophysical principles orchestrating these reaction arrays limits the exploitation of NRPSs in synthetic biology. Here, we use nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry to solve the conundrum of how intermodular recognition is coupled with loaded carrier protein specificity in the tomaymycin NRPS. We discover an adaptor domain that directly recruits the loaded carrier protein from the initiation module to the elongation module and reveal its mechanism of action. The adaptor domain of the type found here has specificity rules that could potentially be exploited in the design of engineered NRPS machinery.

The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.,Karanth MN, Kirkpatrick JP, Krausze J, Schmelz S, Scrima A, Carlomagno T Sci Adv. 2024 Jun 21;10(25):eadm9404. doi: 10.1126/sciadv.adm9404. Epub 2024 Jun , 19. PMID:38896613<ref>PMID:38896613</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8qnf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces regensis]]
[[Category: Carlomagno T]]
[[Category: Karanth M]]
[[Category: Kirkpatrick J]]
[[Category: Krausze J]]
[[Category: Schmelz S]]
[[Category: Scrima A]]