Architecture of full-length type I modular polyketide synthases revealed by X-ray crystallography, cryo-electron microscopy, and AlphaFold2-Reference-Cited by-同舟云学术

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Architecture of full-length type I modular polyketide synthases revealed by X-ray crystallography, cryo-electron microscopy, and AlphaFold2

Published:2024 Issue:8 Volume:41 Page:1219-1234
ISSN:0265-0568
Container-title:Natural Product Reports
language:en
Short-container-title:Nat. Prod. Rep.

Author:

Bagde Saket R.¹²^ORCID,Kim Chu-Young³^ORCID

Affiliation:

1. Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA

2. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA

3. Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA

Abstract

Structures of intact polyketide synthase modules reveal conformational rearrangements and suggest asynchronous use of reaction chambers.

Funder

National Institute of General Medical Sciences

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/NP/D3NP00060E

Reference54 articles.

1. Natural Products as Sources of New Drugs over the Nearly Four Decades from 01/1981 to 09/2019

2. Modular organization of genes required for complex polyketide biosynthesis

3. Modular polyketide synthase contains two reaction chambers that operate asynchronously

4. Mapping the catalytic conformations of an assembly-line polyketide synthase module

5. Routine single particle CryoEM sample and grid characterization by tomography

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