Biochemical and structural characterization of a tail-spike protein with depolymerase activity identified in a marine podovirus.

Sirigu S, Roret T, Mocaër PY, Larocque R, Jouanneau D, Legrand P, Baudoux AC, Czjzek M Acta Crystallogr D Struct Biol (2026) Europe PMC

SASDYY6 – trimeric chaperon domain D4 of depolymerase Dpo31

chaperon for trimerisation of Dpo31
MWI(0) 54 kDa
MWexpected 54 kDa
VPorod 66 nm3
log I(s) 7.03×10-2 7.03×10-3 7.03×10-4 7.03×10-5
chaperon for trimerisation of Dpo31 small angle scattering data  s, nm-1
ln I(s)
chaperon for trimerisation of Dpo31 Guinier plot ln 7.03×10-2 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
chaperon for trimerisation of Dpo31 Kratky plot 1.104 0 √3 sRg
p(r)
chaperon for trimerisation of Dpo31 pair distance distribution function Rg: 2.5 nm 0 Dmax: 6.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
chaperon for trimerisation of Dpo31 GASBOR model
log I(s)
 s, nm-1
chaperon for trimerisation of Dpo31 COOT model
Synchrotron SAXS data from solutions of trimeric chaperon domain D4 of depolymerase Dpo31 in Tris-HCl 50 mM pH 8, NaCl 100 mM, pH 8 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a AVIEX PCCD170170 detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 1.033 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 70.00 μl sample at 9.9 mg/ml was injected at a 0.20 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 15°C. 250 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.

chaperon for trimerisation of Dpo31 (Dpo31-D4)
Mol. type   Protein
Organism   Cobetia phage Carin1
Olig. state   Trimer
Mon. MW   18 kDa
Sequence   FASTA