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

SASDUH7 – Lcl C-terminal domain R477A mutant - trimer

HbP1 (R477A)
MWexperimental 47 kDa
MWexpected 55 kDa
VPorod 79 nm3
log I(s) 9.12×10-2 9.12×10-3 9.12×10-4 9.12×10-5
HbP1 (R477A) small angle scattering data  s, nm-1
ln I(s)
HbP1 (R477A) Guinier plot ln 9.12×10-2 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
HbP1 (R477A) Kratky plot 1.104 0 3 sRg
p(r)
HbP1 (R477A) pair distance distribution function Rg: 2.8 nm 0 Dmax: 9.4 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Lcl C-terminal domain R477A mutant - trimer 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 (R477A) (Lcl-CTD R477A)
Mol. type   Protein
Organism   Legionella pneumophila
Olig. state   Trimer
Mon. MW   18.5 kDa
 
UniProt   E7BLH6 (387-536)
Sequence   FASTA