Mapping the catalytic conformations of an assembly-line polyketide synthase module-Reference-Cited by-同舟云学术

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

Published:2021-11-05 Issue:6568 Volume:374 Page:729-734
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Cogan Dillon P.¹^ORCID,Zhang Kaiming²³^ORCID,Li Xiuyuan¹^ORCID,Li Shanshan²³^ORCID,Pintilie Grigore D.²,Roh Soung-Hun²⁴^ORCID,Craik Charles S.⁵^ORCID,Chiu Wah²⁶^ORCID,Khosla Chaitan¹⁷⁸^ORCID

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, CA 94305, USA.

2. Department of Bioengineering, Stanford University, Stanford, CA 94305, USA.

3. MOE Key Laboratory for Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China.

4. Department of Biological Sciences, Institute of Molecular Biology & Genetics, Seoul National University, Seoul 151-742, Korea.

5. Department of Pharmaceutical Chemistry, University of California–San Francisco, San Francisco, CA 94158, USA.

6. Division of CryoEM and Bioimaging, Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, USA.

7. Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA.

8. Stanford ChEM-H, Stanford, CA 94305, USA.

Abstract

Big molecules build small Actinomycete bacteria are prolific producers of bioactive small molecules such as polyketide antibiotics. These molecules are built by the addition of short carbon units to a growing, protein-tethered chain, either iteratively as in fatty acid synthesis or in a modular fashion by a hand-off from one distinct enzyme complex to the next. Bagde et al . and Cogan et al . report structures of polyketide synthase modules in action, taking advantage of antibody stabilization of one of the domains. Both groups visualized multiple conformational states and an asymmetric arrangement of domains, providing insight into how these molecular assembly machines transfer substrates from one active site to another. —MAF

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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