4xrt
From Proteopedia
(Difference between revisions)
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<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=4xrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xrt OCA], [http://pdbe.org/4xrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xrt RCSB], [http://www.ebi.ac.uk/pdbsum/4xrt PDBsum]</span></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=4xrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xrt OCA], [http://pdbe.org/4xrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xrt RCSB], [http://www.ebi.ac.uk/pdbsum/4xrt PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aromatic polyketides make up a large class of natural products with diverse bioactivity. During biosynthesis, linear poly-beta-ketone intermediates are regiospecifically cyclized, yielding molecules with defined cyclization patterns that are crucial for polyketide bioactivity. The aromatase/cyclases (ARO/CYCs) are responsible for regiospecific cyclization of bacterial polyketides. The two most common cyclization patterns are C7-C12 and C9-C14 cyclizations. We have previously characterized three monodomain ARO/CYCs: ZhuI, TcmN, and WhiE. The last remaining uncharacterized class of ARO/CYCs is the di-domain ARO/CYCs, which catalyze C7-C12 cyclization and/or aromatization. Di-domain ARO/CYCs can further be separated into two subclasses: "nonreducing" ARO/CYCs, which act on nonreduced poly-beta-ketones, and "reducing" ARO/CYCs, which act on cyclized C9 reduced poly-beta-ketones. For years, the functional role of each domain in cyclization and aromatization for di-domain ARO/CYCs has remained a mystery. Here we present what is to our knowledge the first structural and functional analysis, along with an in-depth comparison, of the nonreducing (StfQ) and reducing (BexL) di-domain ARO/CYCs. This work completes the structural and functional characterization of mono- and di-domain ARO/CYCs in bacterial type II polyketide synthases and lays the groundwork for engineered biosynthesis of new bioactive polyketides. | ||
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| + | Structural and functional analysis of two di-domain aromatase/cyclases from type II polyketide synthases.,Caldara-Festin G, Jackson DR, Barajas JF, Valentic TR, Patel AB, Aguilar S, Nguyen M, Vo M, Khanna A, Sasaki E, Liu HW, Tsai SC Proc Natl Acad Sci U S A. 2015 Dec 2. pii: 201512976. PMID:26631750<ref>PMID:26631750</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4xrt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:47, 16 December 2015
Crystal structure of the di-domain ARO/CYC StfQ from the steffimycin biosynthetic pathway
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Categories: Aguilar, S | Barajas, J F | Caldara-Festin, G M | Jackson, D R | Khanna, A | Liu, H W | Nguyen, M | Patel, A | Sasaki, E | Tsai, S C | Valentic, T R | Vo, M | Aro/cyc | Aromatase/cyclase | Dehydratase | Helix-grip fold | Lyase | Natural product | Polyketide | Polyketide synthase
