4y1b
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Structure of crotonyl-CoA carboxylase/reductase AntE V350A in complex with NADP== |
+ | <StructureSection load='4y1b' size='340' side='right' caption='[[4y1b]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4y1b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y1B FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y0k|4y0k]]</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y1b OCA], [http://pdbe.org/4y1b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y1b RCSB], [http://www.ebi.ac.uk/pdbsum/4y1b PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Bioengineering of natural product biosynthesis is a powerful approach to expand the structural diversity of bioactive molecules. However, in polyketide biosynthesis, the modification of polyketide extender units, which form the carbon skeletons, has remained challenging. Herein, we report the rational control of polyketide extender units by the structure-based engineering of a crotonyl-CoA carboxylase/reductase (CCR), in the biosynthesis of antimycin. Site-directed mutagenesis of the CCR enzyme AntE, guided by the crystal structure solved at 1.5 A resolution, expanded its substrate scope to afford indolylmethylmalonyl-CoA by the V350G mutation. The mutant A182L selectively catalyzed carboxylation over the regular reduction. Furthermore, the combinatorial biosynthesis of heterocycle- and substituted arene-bearing antimycins was achieved by an engineered Streptomyces strain bearing AntE(V350G) . These findings deepen our understanding of the molecular mechanisms of the CCRs, which will serve as versatile biocatalysts for the manipulation of building blocks, and set the stage for the rational design of polyketide biosynthesis. | ||
- | + | Rational Control of Polyketide Extender Units by Structure-Based Engineering of a Crotonyl-CoA Carboxylase/Reductase in Antimycin Biosynthesis.,Zhang L, Mori T, Zheng Q, Awakawa T, Yan Y, Liu W, Abe I Angew Chem Int Ed Engl. 2015 Nov 2;54(45):13462-5. doi: 10.1002/anie.201506899., Epub 2015 Sep 10. PMID:26356484<ref>PMID:26356484</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 4y1b" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Abe, I]] | [[Category: Abe, I]] | ||
[[Category: Mori, T]] | [[Category: Mori, T]] | ||
[[Category: Zhang, L]] | [[Category: Zhang, L]] | ||
+ | [[Category: Antimycin biosynthesis]] | ||
+ | [[Category: Carboxylase]] | ||
+ | [[Category: Oxidoreductase]] | ||
+ | [[Category: Transferase]] |
Revision as of 18:49, 30 November 2015
Structure of crotonyl-CoA carboxylase/reductase AntE V350A in complex with NADP
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