Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product.

Dunne M, Leicht S, Krichel B, Mertens HD, Thompson A, Krijgsveld J, Svergun DI, Gómez-Torres N, Garde S, Uetrecht C, Narbad A, Mayer MJ, Meijers R, J Biol Chem 291(10):4882-93 (2016) Europe PMC

SASDAE7 – Structure of a complex between full length and truncated CS74L endolysin

Endolysin CS74L
MWI(0) 38 kDa
MWexpected 31 kDa
VPorod 79 nm3
log I(s) 5.03×101 5.03×100 5.03×10-1 5.03×10-2
Endolysin CS74L small angle scattering data  s, nm-1
ln I(s)
Endolysin CS74L Guinier plot ln 5.03×101 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Endolysin CS74L Kratky plot 1.104 0 √3 sRg
p(r)
Endolysin CS74L pair distance distribution function Rg: 3.8 nm 0 Dmax: 14 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Endolysin CS74L DAMMIF model
log I(s)
 s, nm-1
Endolysin CS74L EOM/RANCH model
Endolysin CS74L EOM/RANCH model
Endolysin CS74L EOM/RANCH model
Synchrotron SAXS data from solutions of Structure of a complex between full length and truncated CS74L endolysin in 20 mM HEPES, pH 7.4 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 6.8 mg/ml were measured at 20°C. Eight successive 15 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Storage temperature = UNKNOWN

Tags: X33
Endolysin CS74L (CS74L)
Mol. type   Protein
Organism   Clostridium phage phi8074-B1
Olig. state   Other
Mon. MW   31.1 kDa
 
UniProt   I1TJX3 (1-264)
Sequence   FASTA