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

Afsar M, Shukla A, Kumar N, Ramachandran R
Acta Crystallographica Section D Structural Biology 77(6) (2021 May 14)

doi: 10.1107/S2059798321003107

Submitted to SASBDB: 2019 Sep 5 Published in SASBDB: 2021 May 18

SASDEU5 – Adenylation domain of DNA ligase A Sample: DNA ligase A monomer, 38 kDa Mycobacterium tuberculosis protein Buffer: 50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8 Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2018 Sep 27 RgGuinier 2.4 nm Dmax 8.8 nm VolumePorod 69 nm3

SASDEC6 – Adenylation Domain of DNA ligase A with NAD+ Sample: DNA ligase A monomer, 38 kDa Mycobacterium tuberculosis protein Buffer: 50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8 Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2018 Oct 6 RgGuinier 2.4 nm Dmax 6.2 nm VolumePorod 94 nm3

SASDG65 – Adenylation domain of DNA ligase A (LigA) Sample: DNA ligase A monomer, 37 kDa Mycobacterium tuberculosis protein Buffer: 50 mM Tris-HCl 200 mM NaCl 2mM β-mercaptoethanol, pH: 8 Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 May 21 RgGuinier 2.7 nm Dmax 8.9 nm VolumePorod 68 nm3