한빛사
>
한빛사논문
한빛사논문
- 조회260
Nat. Prod. Rep., Mar 19 2024, | https://doi.org/10.1039/d3np00060e
Architecture of full-length type I modular polyketide synthases revealed by X-ray crystallography, cryo-electron microscopy, and AlphaFold2
Saket R. Bagde ab and Chu-Young Kim *c
aProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA
bDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA
cDepartment of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA
*Corresponding authors : Chu-Young Kim
Abstract
Covering: up to the end of 2023Type I modular polyketide synthases construct polyketide natural products in an assembly line-like fashion, where the growing polyketide chain attached to an acyl carrier protein is passed from catalytic domain to catalytic domain. These enzymes have immense potential in drug development since they can be engineered to produce non-natural polyketides by strategically adding, exchanging, and deleting individual catalytic domains. In practice, however, this approach frequently results in complete failures or dramatically reduced product yields. A comprehensive understanding of modular polyketide synthase architecture is expected to resolve these issues. We summarize the three-dimensional structures and the proposed mechanisms of three full-length modular polyketide synthases, Lsd14, DEBS module 1, and PikAIII. We also describe the advantages and limitations of using X-ray crystallography, cryo-electron microscopy, and AlphaFold2 to study intact type I polyketide synthases.
논문정보
- Review Paper
- 2024년 03월 (BRIC 등록일 2024-04-05)
- 국외 연구진
- 생명과학 > 분자생물학
댓글 작성 로그인
팝업 닫기관련 링크
연구자 키워드
관련분야 연구자보기
소속기관 논문보기
관련분야 논문보기
해당논문 저자보기
