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
BON domain protein Kratky plot 1.104 0 3 sRg
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