Structure and analysis of a virulent chitinase from Listeria monocytogenes.

Rehman S, Baczynska M, Zhang B, Lorenz CD, Garnett JA, Biochim Biophys Acta Proteins Proteom :141106 (2025) Europe PMC

SASDWK5 – Listeria monocytogenes Chitinase (ChiA)

chitinase
MWexperimental 36 kDa
MWexpected 36 kDa
VPorod 58 nm3
log I(s) 6.15×10-2 6.15×10-3 6.15×10-4 6.15×10-5
chitinase small angle scattering data  s, nm-1
ln I(s)
chitinase Guinier plot ln 6.15×10-2 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
chitinase Kratky plot 1.104 0 √3 sRg
p(r)
chitinase pair distance distribution function Rg: 2.1 nm 0 Dmax: 5.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
chitinase REFMAC model
Synchrotron SAXS data from solutions of Listeria monocytogenes Chitinase (ChiA) in 20 mM Tris, 200 mM NaCl, pH 8 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a wavelength of λ = 1 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 50.00 μl sample at 10 mg/ml was injected at a 0.16 ml/min flow rate onto a Shodex KW403-4F column at 25°C. 620 successive 0.500 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.

Sample detector distance = UNKNOWN

chitinase (ChiA)
Mol. type   Protein
Organism   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Olig. state   Monomer
Mon. MW   36.5 kDa
 
UniProt   Q8Y619 (30-352)
Sequence   FASTA