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

SASDNQ9 – Acyltransferase domain of polyketide synthase Pks13 at neutral pH

Polyketide synthase Pks13
MWI(0) 54 kDa
MWexpected 51 kDa
VPorod 85 nm3
log I(s) 1.11×10-1 1.11×10-2 1.11×10-3 1.11×10-4
Polyketide synthase Pks13 small angle scattering data  s, nm-1
ln I(s)
Polyketide synthase Pks13 Guinier plot ln 1.11×10-1 Rg: 2.8 nm 0 (2.8 nm)-2 s2
Polyketide synthase Pks13 Kratky plot 1.104 0 3 sRg
Polyketide synthase Pks13 pair distance distribution function Rg: 2.7 nm 0 Dmax: 8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Polyketide synthase Pks13 DAMMIN model

Synchrotron SAXS data from solutions of the acyltransferase domain of polyketide synthase Pks13 at neutral pH in 50 mM Tris-HCl, 300 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 12°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 (fAT-acyltransferase)
Mol. type   Protein
Organism   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Olig. state   Monomer
Mon. MW   51.2 kDa
UniProt   I6X8D2 (591-1046)
Sequence   FASTA