Structural and biophysical characterization of Mycobacterium tuberculosis DciA reveals functional convergence in DnaB helicase recognition.

Mazzoletti D, Garavaglia A, Fisher H Gao N, Morrone C, Olinares PDB, Chait BT, Jeruzalmi D, Miggiano R, Protein Sci 35(9):e70771 (2026) Europe PMC

SASDYU2 – DNA replication protein DciA from M.turberculosis

DNA replication protein DciA
MWexperimental 21 kDa
MWexpected 21 kDa
VPorod 36 nm3
log I(s) 7.87×100 7.87×10-1 7.87×10-2 7.87×10-3
DNA replication protein DciA small angle scattering data  s, nm-1
ln I(s)
DNA replication protein DciA Guinier plot ln 7.88×100 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
DNA replication protein DciA Kratky plot 1.104 0 √3 sRg
p(r)
DNA replication protein DciA pair distance distribution function Rg: 3.5 nm 0 Dmax: 14.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
DNA replication protein DciA OTHER model
log I(s)
 s, nm-1
DNA replication protein DciA OTHER model
Synchrotron SAXS data from solutions of DNA replication protein DciA from M.turberculosis in 20 mM HEPES, 300 mM NaCl, 2mM b-Me, 5% glycerol, pH 7.5 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 4.3 mg/ml was injected at a 0.50 ml/min flow rate onto a Agilent AdvanceBio SEC 300Å, 4.6 x 150 mm column at 20°C. 1600 successive 2 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 replication protein DciA (MtDciA)
Mol. type   Protein
Organism   Mycobacterium tuberculosis
Olig. state   Monomer
Mon. MW   21.0 kDa
Sequence   FASTA