Decrypting the oscillating nature of the 4′-phosphopantetheine arm in acyl carrier protein AcpM of Mycobacteriumtuberculosis

FEBS Letters

article

Rupam Biswas¹  Bina Kumari Singh²  Debajyoti Dutta¹  Prabir Kumar Das¹  Mrinal Kumar Maiti¹  Amit Basak²  Amit Kumar Das¹ 

[1] Department of Biotechnology, Indian Institute of Technology;School of Biosciences, Indian Institute of Technology;Department of Chemistry, Indian Institute of Technology

关键词: acyl carrier protein;    coenzyme A;    fatty acid synthase;    fluorescence spectroscopy;    molecular dynamics;    Mycobacterium tuberculosis;    ;   

DOI  :  10.1002/1873-3468.13339

来源: John Wiley & Sons Ltd.

【 摘 要 】

In Mycobacterium tuberculosis, acyl carrier protein (AcpM)-mediated fatty acid synthase type II is integral for the synthesis of mycolic acids. AcpM, designated as an atypical ACP, comprises of a putative 33 amino acid long C-terminal extension which is distinctive in nature. Here, we aimed at devising an ‘easy-to-go’ method for the generation of crypto-AcpM loaded with a solvatochromic probe 7-Nitrobenz-2-oxa-1,3-diazol-4-yl, which is linked to the 40 -phosphopantetheine (Ppant) prosthetic group of AcpM. The cryptoAcpM, coupled with fluorescence spectroscopy and molecular dynamics simulation studies, was employed to explore the elusive dynamics of Ppant arm in AcpM. This investigation establishes the role of the flexible C-terminal extension of AcpM in regulating the prosthetic group sequestration ability by modulating the ‘Asp-Ser-Leu’ motif.

【 授权许可】

Unknown