7uwr
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==KSQ+AT from first module of the pikromycin synthase== | |
| + | <StructureSection load='7uwr' size='340' side='right'caption='[[7uwr]], [[Resolution|resolution]] 2.61Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7uwr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UWR FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.61Å</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=7uwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uwr OCA], [https://pdbe.org/7uwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uwr RCSB], [https://www.ebi.ac.uk/pdbsum/7uwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uwr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The first domain of modular polyketide synthases (PKSs) is most commonly a ketosynthase (KS)-like enzyme, KS(Q), that primes polyketide synthesis. Unlike downstream KSs that fuse alpha-carboxyacyl groups to growing polyketide chains, it performs an extension-decoupled decarboxylation of these groups to generate primer units. When Pik127, a model triketide synthase constructed from modules of the pikromycin synthase, was studied by cryoelectron microscopy (cryo-EM), the dimeric didomain comprised of KS(Q) and the neighboring methylmalonyl-selective acyltransferase (AT) dominated the class averages and yielded structures at 2.5- and 2.8-A resolution, respectively. Comparisons with ketosynthases complexed with their substrates revealed the conformation of the (2S)-methylmalonyl-S-phosphopantetheinyl portion of KS(Q) and KS substrates prior to decarboxylation. Point mutants of Pik127 probed the roles of residues in the KS(Q) active site, while an AT-swapped version of Pik127 demonstrated that KS(Q) can also decarboxylate malonyl groups. Mechanisms for how KS(Q) and KS domains catalyze carbon-carbon chemistry are proposed. | ||
| - | + | Priming enzymes from the pikromycin synthase reveal how assembly-line ketosynthases catalyze carbon-carbon chemistry.,Dickinson MS, Miyazawa T, McCool RS, Keatinge-Clay AT Structure. 2022 Sep 1;30(9):1331-1339.e3. doi: 10.1016/j.str.2022.05.021. Epub , 2022 Jun 22. PMID:35738283<ref>PMID:35738283</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Dickinson | + | <div class="pdbe-citations 7uwr" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces venezuelae]] | ||
| + | [[Category: Dickinson MS]] | ||
| + | [[Category: Keatinge-Clay AT]] | ||
| + | [[Category: McCool RS]] | ||
| + | [[Category: Miyazawa T]] | ||
Current revision
KSQ+AT from first module of the pikromycin synthase
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