Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis.
FadD28 from Mycobacterium tuberculosis belongs to the fatty-acyl AMP ligase (FAAL) family of proteins. It is essential for the biosynthesis of a virulent phthiocerol dimycocerosate (PDIM) lipid that is only found in the cell wall of pathogenic mycobacteria. The N-terminal domain, comprising of the first 460 residues, was crystallized by the hanging-drop vapour-diffusion method at 295 K. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 angstroms. The crystal structure of the N-terminal domain of FadD28 at 2.35 angstroms resolution has been solved using the MAD method.
Goyal
Aneesh
A
Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500007, India.
Yousuf
Malikmohamed
M
Rajakumara
Eerappa
E
Arora
Pooja
P
Gokhale
Rajesh S
RS
Sankaranarayanan
Rajan
R
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D019730:Carbon-Sulfur Ligases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D010446:Peptide Fragments / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D001426:Bacterial Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D019730:Carbon-Sulfur Ligases; C510957:FadD28 protein, Mycobacterium tuberculosis