Decrypting the oscillating nature of the 4′‐phosphopantetheine arm in acyl carrier protein AcpM of Mycobacterium tuberculosis
Author:
Affiliation:
1. Department of Biotechnology Indian Institute of Technology, Kharagpur India
2. School of Biosciences Indian Institute of Technology, Kharagpur India
3. Department of Chemistry Indian Institute of Technology, Kharagpur India
Funder
Department of Biotechnology , Ministry of Science and Technology
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.13339
Reference40 articles.
1. Structure of a modular polyketide synthase
2. Current understanding of fatty acid biosynthesis and the acyl carrier protein
3. Structural Biology of Nonribosomal Peptide Synthetases
4. Structure and Conformational Variability of the Mycobacterium tuberculosis Fatty Acid Synthase Multienzyme Complex
5. THE STRUCTURAL BIOLOGY OF TYPE II FATTY ACID BIOSYNTHESIS
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1. The C‐terminal end of mycobacterial HadBC regulates AcpM interaction during the FAS‐II pathway: a structural perspective;The FEBS Journal;2022-03-23
2. Mycobacterial crypto-AcpM as a tool to investigate the consequence of drug binding on its key FAS II partner enzyme HadAB;Biochimica et Biophysica Acta (BBA) - General Subjects;2021-10
3. L. major apo-acyl carrier protein forms ordered aggregates due to an exposed phenylalanine, while phosphopantetheine inhibits aggregation in the holo-form;International Journal of Biological Macromolecules;2021-05
4. A Single Tool to Monitor Multiple Protein–Protein Interactions of the Escherichia coli Acyl Carrier Protein;ACS Infectious Diseases;2019-07-18
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