The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans.

Rehman S, Antonovic AK, McIntire IE, Zheng H, Cleaver L, Baczynska M, Adams CO, Portlock T, Richardson K, Shaw R, Oregioni A, Mastroianni G, Whittaker SB, Kelly G, Lorenz CD, Fornili A, Cianciotto NP, Garnett JA, Nat Commun 15(1):4912 (2024) Europe PMC

SASDUG7 – Wild type Lcl C-terminal domain

HbP1
MWexperimental 51 kDa
MWexpected 56 kDa
VPorod 105 nm3
log I(s) 9.03×10-2 9.03×10-3 9.03×10-4 9.03×10-5
HbP1 small angle scattering data  s, nm-1
ln I(s)
HbP1 Guinier plot ln 9.04×10-2 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
HbP1 Kratky plot 1.104 0 √3 sRg
p(r)
HbP1 pair distance distribution function Rg: 2.9 nm 0 Dmax: 9.7 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Wild type Lcl C-terminal domain in 20 mM Tris–HCl pH 8.0, 200 mM NaCl, 5 mM EDTA were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Pilatus 2M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 25°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

HbP1 (Lcl-CTD WT)
Mol. type   Protein
Organism   Legionella pneumophila
Olig. state   Trimer
Mon. MW   18.5 kDa
 
UniProt   E7BLH6 (387-536)
Sequence   FASTA