loading page

The Crystal Structure of AbsH3: a Putative FAD-dependent Reductase in the Abyssomicin Biosynthesis Pathway.
  • +6
  • Jonathan Clinger,
  • Xiachang Wang,
  • Wenlong Cai,
  • Yanyan Zhu,
  • Mitchell Miller,
  • Chang-Guo Zhan,
  • Steven Van Lanen,
  • Jon Thorson,
  • George Phillips
Jonathan Clinger
Rice University
Author Profile
Xiachang Wang
University of Kentucky
Author Profile
Wenlong Cai
University of Kentucky
Author Profile
Yanyan Zhu
University of Kentucky
Author Profile
Mitchell Miller
Rice University
Author Profile
Chang-Guo Zhan
University of Kentucky
Author Profile
Steven Van Lanen
University of Kentucky
Author Profile
Jon Thorson
University of Kentucky
Author Profile
George Phillips
Rice University
Author Profile

Peer review status:IN REVISION

09 Feb 2020Submitted to PROTEINS: Structure, Function, and Bioinformatics
04 May 2020Submission Checks Completed
04 May 2020Assigned to Editor
15 May 2020Reviewer(s) Assigned
22 May 2020Review(s) Completed, Editorial Evaluation Pending
28 May 2020Editorial Decision: Revise Minor
18 Jun 20201st Revision Received
02 Jul 2020Assigned to Editor
02 Jul 2020Submission Checks Completed

Abstract

Natural products and natural product-derived compounds have been widely used for pharmaceuticals for many years, and the search for new natural products that may have interesting activity is on going. Abyssomicins are natural product molecules that have antibiotic activity via inhibition of the folate synthesis pathway in microbiota. These compounds also appear to undergo a required [4+2] cycloaddition in their biosynthetic pathway. Here we report the structure of an FAD-dependent reductase, AbsH3, from the biosynthetic gene cluster of novel abyssomicins found in Streptomyces sp. LC-6-2.