The NMR solution structure of Mycobacterium tuberculosis F-ATP synthase subunit ε provides new insight into energy coupling inside the rotary engine

• Main Authors: Joon, Shin, Ragunathan, Priya, Sundararaman, Lavanya, Nartey, Wilson, Kundu, Subhashri, Manimekalai, Malathy Sony Subramanian, Bogdanović, Nebojša, Dick, Thomas, Grüber, Gerhard
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2020
• Subjects: Science::Biological sciences::Biophysics; Science::Biological sciences::Biochemistry; Bioenergetics; F-ATP Synthase
• Online Access: https://hdl.handle.net/10356/138820
• Institution: Nanyang Technological University

Mycobacterium tuberculosis (Mt) F1F0 ATP synthase (α3:β3:γ:δ:ε:a:b:b′:c9) is essential for the viability of growing and nongrowing persister cells of the pathogen. Here, we present the first NMR solution structure of Mtε, revealing an N‐terminal β‐barrel domain (NTD) and a C‐terminal domain (CTD) co...