Crystal Structure of the Brugia malayi Thymidylate Kinase-dTMP Complex and Small Angle X-ray Scattering Experiments Identifies Changes in the Dimeric Association Compared to the Human Homolog

Vishwakarma J, Sharma V, Kumar S, Ramachandran R, Crystallography Reports 68(7):1150-1158 (2024) DOI

SASDKU9 – Thymidylate kinase (dTMP kinase) at pH 8.0

dTMP kinase
MWexperimental 50 kDa
MWexpected 57 kDa
VPorod 81 nm3
log I(s) 1.47×105 1.47×104 1.47×103 1.47×102
dTMP kinase small angle scattering data  s, nm-1
ln I(s)
dTMP kinase Guinier plot ln 1.47×105 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
dTMP kinase Kratky plot 1.104 0 √3 sRg
p(r)
dTMP kinase pair distance distribution function Rg: 3.0 nm 0 Dmax: 8.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
dTMP kinase GASBOR model
log I(s)
 s, nm-1
dTMP kinase DAMMIF model
SAXS data from solutions of thymidylate kinase in 20 mM Tris, 150 mM NaCl, pH 8 were collected using an Anton Paar SAXSpace instrument equipped with a Mythen2 R 1K detector (CSIR-Central Drug Research Institute, Lucknow, India) at a sample-detector distance of 0.317 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 9.00 mg/ml was measured. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Experimental temperature: UNKNOWN. X-ray exposure time: UNKNOWN.

dTMP kinase (TMK)
Mol. type   Protein
Organism   Brugia malayi
Olig. state   Dimer
Mon. MW   28.3 kDa
 
UniProt   A0A1P6BP23 (1-213)
Sequence   FASTA