BonA from Acinetobacter baumannii Forms a Divisome-Localized Decamer That Supports Outer Envelope Function.

Grinter R Morris FC, Dunstan RA, Leung PM, Kropp A, Belousoff M, Gunasinghe SD, Scott NE, Beckham S, Peleg AY, Greening C, Li J, Heinz E, Lithgow T, mBio :e0148021 (2021) Europe PMC

SASDJX3 – YraP from Acinetobacter baumannii full-length, minus signal-peptide and 27 N-terminal amino acids

BON domain protein
MWexperimental 29 kDa
MWexpected 20 kDa
VPorod 49 nm3
log I(s) 4.89×10-2 4.89×10-3 4.89×10-4 4.89×10-5
BON domain protein small angle scattering data  s, nm-1
ln I(s)
BON domain protein Guinier plot ln 4.89×10-2 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
BON domain protein Kratky plot 1.104 0 √3 sRg
p(r)
BON domain protein pair distance distribution function Rg: 3.2 nm 0 Dmax: 10.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
BON domain protein DAMMIF model
log I(s)
 s, nm-1
BON domain protein DAMMIF model
Synchrotron SAXS data from solutions of N-terminal truncated YraP from Acinetobacter baumannii in 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH 7.8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.10322 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 10.7 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 11 successive 0.100 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.

BON domain protein (YraP (46-235))
Mol. type   Protein
Organism   Acinetobacter baumannii
Olig. state   Monomer
Mon. MW   20.4 kDa
 
UniProt   V5VFJ0 (46-235)
Sequence   FASTA