Structure of the lantibiotic dehydratase MadB

Jens Reiners.

SASDRX6 – lantibiotic dehydratase MadB (apo)

Thiopeptide-type bacteriocin biosynthesis domain containing protein
MWexperimental 243 kDa
MWexpected 250 kDa
VPorod 440 nm3
log I(s) 1.18×10-1 1.18×10-2 1.18×10-3 1.18×10-4
Thiopeptide-type bacteriocin biosynthesis domain containing protein small angle scattering data  s, nm-1
ln I(s)
Thiopeptide-type bacteriocin biosynthesis domain containing protein Guinier plot ln 1.18×10-1 Rg: 4.5 nm 0 (4.5 nm)-2 s2
(sRg)2I(s)/I(0)
Thiopeptide-type bacteriocin biosynthesis domain containing protein Kratky plot 1.104 0 √3 sRg
p(r)
Thiopeptide-type bacteriocin biosynthesis domain containing protein pair distance distribution function Rg: 4.3 nm 0 Dmax: 13.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Thiopeptide-type bacteriocin biosynthesis domain containing protein GASBOR model
Synchrotron SAXS data from solutions of lantibiotic dehydratase MadB in 50 mM HEPES, 200 mM NaCl, 1 % (v/v) glycerol, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 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 100.00 μl sample at 6 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 15°C. 3000 successive 0.995 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.

Thiopeptide-type bacteriocin biosynthesis domain containing protein (MadB)
Mol. type   Protein
Organism   Clostridium sp. Maddingley MBC34-26
Olig. state   Dimer
Mon. MW   124.9 kDa
 
UniProt   K6TUQ9 (1-1038)
Sequence   FASTA