6kxd
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6kxd is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The ishigamide ketosynthase/chain length factor== |
| + | <StructureSection load='6kxd' size='340' side='right'caption='[[6kxd]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6kxd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._MSC090213JE08 Streptomyces sp. MSC090213JE08]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KXD 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]] 1.75Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6kxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kxd OCA], [https://pdbe.org/6kxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kxd RCSB], [https://www.ebi.ac.uk/pdbsum/6kxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kxd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1Y1BW67_9ACTN A0A1Y1BW67_9ACTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In type II polyketide synthases (PKSs), the ketosynthase-chain length factor (KS-CLF) complex catalyzes polyketide chain elongation with the acyl carrier protein (ACP). Highly reducing type II PKSs, represented by IgaPKS, produce polyene structures instead of the well-known aromatic skeletons. Here, we report the crystal structures of the Iga11-Iga12 (KS-CLF) heterodimer and the covalently cross-linked Iga10=Iga11-Iga12 (ACP=KS-CLF) tripartite complex. The latter structure revealed the molecular basis of the interaction between Iga10 and Iga11-Iga12, which differs from that between the ACP and KS of Escherichia coli fatty acid synthase. Furthermore, the reaction pocket structure and site-directed mutagenesis revealed that the negative charge of Asp 113 of Iga11 prevents further condensation using a beta-ketoacyl product as a substrate, which distinguishes IgaPKS from typical type II PKSs. This work will facilitate the future rational design of PKSs. | ||
| - | + | Structural basis for selectivity in a highly reducing type II polyketide synthase.,Du D, Katsuyama Y, Horiuchi M, Fushinobu S, Chen A, Davis TD, Burkart MD, Ohnishi Y Nat Chem Biol. 2020 May 4. pii: 10.1038/s41589-020-0530-0. doi:, 10.1038/s41589-020-0530-0. PMID:32367018<ref>PMID:32367018</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6kxd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces sp. MSC090213JE08]] | ||
| + | [[Category: Burkart M]] | ||
| + | [[Category: Chen A]] | ||
| + | [[Category: Davis T]] | ||
| + | [[Category: Du D]] | ||
| + | [[Category: Fushinobu S]] | ||
| + | [[Category: Horiuchi M]] | ||
| + | [[Category: Katsuyama Y]] | ||
| + | [[Category: Ohnishi Y]] | ||
Current revision
The ishigamide ketosynthase/chain length factor
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