Solution structure of the type I polyketide synthase Pks13 from Mycobacterium tuberculosis.

Bon C, Cabantous S, Julien S, Guillet V, Chalut C, Rima J, Brison Y, Malaga W, Sanchez-Dafun A, Gavalda S, Quémard A, Marcoux J, Waldo GS, Guilhot C, Mourey L, BMC Biol 20(1):147 (2022) Europe PMC

SASDNS9 – KS domain of polyketide synthase Pks13 at neutral pH

Polyketide synthase Pks13
MWI(0) 54 kDa
MWexpected 51 kDa
VPorod 82 nm3
log I(s) 2.26×10-2 2.26×10-3 2.26×10-4 2.26×10-5
Polyketide synthase Pks13 small angle scattering data  s, nm-1
ln I(s)
Polyketide synthase Pks13 Guinier plot ln 2.27×10-2 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Polyketide synthase Pks13 Kratky plot 1.104 0 √3 sRg
p(r)
Polyketide synthase Pks13 pair distance distribution function Rg: 2.9 nm 0 Dmax: 10 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Polyketide synthase Pks13 DAMMIN model
Synchrotron SAXS data from solutions of the KS domain of polyketide synthase Pks13 at neutral pH in 50 mM Tris-HCl, 50 mM NaCl, pH 8 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a AVIEX PCCD170170 detector at a wavelength of λ = 0.103 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 40.00 μl sample at 3 mg/ml was injected at a 0.20 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 15°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Sample detector distance = UNKNOWN. Number of frames = UNKNOWN

Polyketide synthase Pks13 (Pks13: KS domain)
Mol. type   Protein
Organism   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Olig. state   Monomer
Mon. MW   50.5 kDa
 
UniProt   I6X8D2 (119-575)
Sequence   FASTA