Structural enzymological studies of the long chain fatty acyl-CoA synthetase FadD5 from the mce1 operon of Mycobacterium tuberculosis.

Rahman MA, Dalwani S, Venkatesan R, Biochem Biophys Res Commun 769:151960 (2025) Europe PMC

SASDX72 – Fatty acyl-CoA synthetase FadD5 with 2 mM coenzyme A (CoA)

Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase)
MWexperimental 127 kDa
MWexpected 123 kDa
VPorod 210 nm3
log I(s) 1.74×10-1 1.74×10-2 1.74×10-3 1.74×10-4
Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase) small angle scattering data  s, nm-1
ln I(s)
Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase) Guinier plot ln 1.75×10-1 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase) Kratky plot 1.104 0 √3 sRg
Dmax: 12 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase) ALPHAFOLD model
Synchrotron SAXS data from solutions of Fatty acyl-CoA synthetase in 20 mM HEPES, 500 mM NaCl, 5 mM MgCl2, 1 mM β-mercaptoethanol, 2 mM coenzyme A (CoA), pH 7.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.72 m and at a wavelength of λ = 0.09537 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured at 4°C. 20 successive 1 s 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.

Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase) (FadD5)
Mol. type   Protein
Organism   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Olig. state   Dimer
Mon. MW   61.7 kDa
 
UniProt   O07411 (1-554)
Sequence   FASTA