|
type |
Journal Article |
authors |
Mani Tripathi S, Ramachandran R.
|
title |
Overexpression, purification and crystallization of lysine epsilon-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv |
journal |
Acta Crystallogr Sect F Struct Biol Cryst Commun |
Activity |
2.6.1.36 |
Family |
2.6.1.36.a |
sel |
selected |
ui |
16754985 |
year |
(2006) |
volume |
62 |
number |
6 |
pages |
572-5 |
| |
abstract |
Lysine epsilon-aminotransferase (LAT) is a protein involved in lysine catabolism; it belongs to the aminotransferase family of enzymes, which use pyridoxal 5'-phosphate (PLP) as a cofactor. LAT probably plays a significant role during the persistent/latent phase of Mycobacterium tuberculosis, as observed by its up-regulation by approximately 40-fold during this stage. Crystals of recombinant LAT have been grown in 0.1 M trisodium citrate dihydrate solution containing 0.2 M ammonium acetate and 25% PEG 4000 in the pH range 5.4-6.0. Diffraction data extending to 1.98 A were collected at room temperature from a single crystal. Crystals are trigonal in shape and belong to space group P3(1)21, with unit-cell parameters a = 103.26, b = 103.26, c = 98.22 A. The crystals contain a monomer in the asymmetric unit, which corresponds to a Matthews coefficient (V(M)) of 3.1 A3 Da(-1). |
last changed |
2011/03/03 09:26 |
|