Structural basis for domain rotation during adenylation of active site K123 and fragment library screening against NAD+ -dependent DNA ligase from Mycobacterium tuberculosis

Structural basis for domain rotation during adenylation of active site K123 and fragment library screening against NAD+ -dependent DNA ligase from Mycobacterium tuberculosis Descriptor: BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE, DNA ligase A, SULFATE ION Authors: Ramachandran, R, Shukla, A, Afsar, M. Deposit date: 2019-08-23 Release date: 2020-08-26 Last modified: 2023-11-22 Method: X-RAY DIFFRACTION (2.5 Å) Cite: Salt bridges at the subdomain interfaces of the adenylation domain and active-site residues of Mycobacterium tuberculosis NAD + -dependent DNA ligase A (MtbLigA) are important for the initial steps of nick-sealing activity. Acta Crystallogr D Struct Biol, 77, 2021