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Title: Structural and Functional Trends in Dehydrating Bimodules from trans -Acyltransferase Polyketide Synthases

Abstract

In an effort to uncover the structural motifs and biosynthetic logic of the relatively uncharacterized trans-acyltransferase polyketide synthases, we have begun the dissection of the enigmatic dehydrating bimodules common in these enzymatic assembly lines. We report the 1.98 Å resolution structure of a ketoreductase (KR) from the first half of a type A dehydrating bimodule and the 2.22 Å resolution structure of a dehydratase (DH) from the second half of a type B dehydrating bimodule. The KR, from the third module of the bacillaene synthase, and the DH, from the tenth module of the difficidin synthase, possess features not observed in structurally characterized homologs. The DH architecture provides clues for how it catalyzes a unique double dehydration. Correlations between the chemistries proposed for dehydrating bimodules and bioinformatic analysis indicate that type A dehydrating bimodules generally produce an α/β-cis alkene moiety, while type B dehydrating bimodules generally produce an α/β-trans, γ/δ-cis diene moiety.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NIHOTHER
OSTI Identifier:
1375350
Resource Type:
Journal Article
Resource Relation:
Journal Name: Structure; Journal Volume: 25; Journal Issue: 7
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Wagner, Drew T., Zeng, Jia, Bailey, Constance B., Gay, Darren C., Yuan, Fang, Manion, Hannah R., and Keatinge-Clay, Adrian T. Structural and Functional Trends in Dehydrating Bimodules from trans -Acyltransferase Polyketide Synthases. United States: N. p., 2017. Web. doi:10.1016/j.str.2017.05.011.
Wagner, Drew T., Zeng, Jia, Bailey, Constance B., Gay, Darren C., Yuan, Fang, Manion, Hannah R., & Keatinge-Clay, Adrian T. Structural and Functional Trends in Dehydrating Bimodules from trans -Acyltransferase Polyketide Synthases. United States. doi:10.1016/j.str.2017.05.011.
Wagner, Drew T., Zeng, Jia, Bailey, Constance B., Gay, Darren C., Yuan, Fang, Manion, Hannah R., and Keatinge-Clay, Adrian T. Sat . "Structural and Functional Trends in Dehydrating Bimodules from trans -Acyltransferase Polyketide Synthases". United States. doi:10.1016/j.str.2017.05.011.
@article{osti_1375350,
title = {Structural and Functional Trends in Dehydrating Bimodules from trans -Acyltransferase Polyketide Synthases},
author = {Wagner, Drew T. and Zeng, Jia and Bailey, Constance B. and Gay, Darren C. and Yuan, Fang and Manion, Hannah R. and Keatinge-Clay, Adrian T.},
abstractNote = {In an effort to uncover the structural motifs and biosynthetic logic of the relatively uncharacterized trans-acyltransferase polyketide synthases, we have begun the dissection of the enigmatic dehydrating bimodules common in these enzymatic assembly lines. We report the 1.98 Å resolution structure of a ketoreductase (KR) from the first half of a type A dehydrating bimodule and the 2.22 Å resolution structure of a dehydratase (DH) from the second half of a type B dehydrating bimodule. The KR, from the third module of the bacillaene synthase, and the DH, from the tenth module of the difficidin synthase, possess features not observed in structurally characterized homologs. The DH architecture provides clues for how it catalyzes a unique double dehydration. Correlations between the chemistries proposed for dehydrating bimodules and bioinformatic analysis indicate that type A dehydrating bimodules generally produce an α/β-cis alkene moiety, while type B dehydrating bimodules generally produce an α/β-trans, γ/δ-cis diene moiety.},
doi = {10.1016/j.str.2017.05.011},
journal = {Structure},
number = 7,
volume = 25,
place = {United States},
year = {Sat Jul 01 00:00:00 EDT 2017},
month = {Sat Jul 01 00:00:00 EDT 2017}
}