M. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair.

Khanam T, Afsar M, Shukla A, Alam F, Kumar S, Soyar H, Dolma K, Pasupuleti M, Srivastava KK, Ampapathi RS, Ramachandran R, Nucleic Acids Res (2020) Europe PMC

SASDDV9 – Mycobacterium tuberculosis DNA LigaseA with Nicked DNA

DNA ligase A
Nicked DNA
MWexperimental 121 kDa
MWexpected 92 kDa
VPorod 262 nm3
log I(s) 1.44×101 1.44×100 1.44×10-1 1.44×10-2
DNA ligase A Nicked DNA small angle scattering data  s, nm-1
ln I(s)
DNA ligase A Nicked DNA Guinier plot ln 1.44×101 Rg: 4.4 nm 0 (4.4 nm)-2 s2
(sRg)2I(s)/I(0)
DNA ligase A Nicked DNA Kratky plot 1.104 0 3 sRg
p(r)
DNA ligase A Nicked DNA pair distance distribution function Rg: 4.5 nm 0 Dmax: 14.8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
DNA ligase A Nicked DNA DAMFILT model

Synchrotron SAXS data from solutions of Mycobacterium tuberculosis DNA LigaseA with nicked DNA in 50 mM Tris-HCl 200 mM NaCl 2mM β-mercaptoethanol, pH 8 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 1.1 m and at a wavelength of λ = 0.081 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.50 mg/ml was measured at 10°C. 10 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

DNA ligase A
Mol. type   Protein
Organism   Mycobacterium tuberculosis
Olig. state   Monomer
Mon. MW   76.1 kDa
 
UniProt   P9WNV1
Sequence   FASTA
 
Nicked DNA
Mol. type   DNA
Olig. state   Dimer
Mon. MW   8.1 kDa
Sequence   FASTA