This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6kxd
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==The ishigamide ketosynthase/chain length factor== | ==The ishigamide ketosynthase/chain length factor== | ||
| - | <StructureSection load='6kxd' size='340' side='right'caption='[[6kxd]]' scene=''> | + | <StructureSection load='6kxd' size='340' side='right'caption='[[6kxd]], [[Resolution|resolution]] 1.75Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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 [http://proteopedia.org/fgij/fg.htm?mol=6KXD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6kxd]] is a 2 chain structure. 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 [http://proteopedia.org/fgij/fg.htm?mol=6KXD FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6kxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kxd OCA], [http://pdbe.org/6kxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kxd RCSB], [http://www.ebi.ac.uk/pdbsum/6kxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kxd ProSAT]</span></td></tr> | + | </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'>[http://proteopedia.org/fgij/fg.htm?mol=6kxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kxd OCA], [http://pdbe.org/6kxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kxd RCSB], [http://www.ebi.ac.uk/pdbsum/6kxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kxd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6kxd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Burkart M]] | + | [[Category: Burkart, M]] |
| - | [[Category: Chen A]] | + | [[Category: Chen, A]] |
| - | [[Category: Davis T]] | + | [[Category: Davis, T]] |
| - | [[Category: Du D]] | + | [[Category: Du, D]] |
| - | [[Category: Fushinobu S]] | + | [[Category: Fushinobu, S]] |
| - | [[Category: Horiuchi M]] | + | [[Category: Horiuchi, M]] |
| - | [[Category: Katsuyama Y]] | + | [[Category: Katsuyama, Y]] |
| - | [[Category: Ohnishi Y]] | + | [[Category: Ohnishi, Y]] |
| + | [[Category: Polyketide synthase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 05:59, 20 May 2020
The ishigamide ketosynthase/chain length factor
| |||||||||||
