Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei.
The bifunctional catalase-peroxidase KatG encoded by the katG gene of Burkholderia pseudomallei has a predicted subunit size of 81.6 kDa. It shows high sequence similarity to other catalase-peroxidases of bacterial, archaebacterial and fungal origin, including 64% identity to KatG from Mycobacterium tuberculosis and lesser sequence similarity to members of the plant peroxidase family. Crystals from this protein were grown in 16-20% PEG 4000, 20% 2-methyl-2,4-pentanediol and 0.1 M sodium citrate pH 5.6 by the hanging-drop vapour-diffusion method at 293 K. These crystals diffracted beyond 1.8 A resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 100.9, b = 115.6, c = 175.2 A. The data are consistent with either a monomer or a dimer in the crystal asymmetric unit.
Carpena
Xavier
X
Institut de Biología Molecular de Barcelona CSIC, Jordi-Girona 18-26, 08034 Barcelona, Spain.
Switala
Jack
J
Loprasert
Suvit
S
Mongkolsuk
Skorn
S
Fita
Ignacio
I
Loewen
Peter C
PC
D001426:Bacterial Proteins; D016957:Burkholderia pseudomallei / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry*; D011487:Protein Conformation
D001426:Bacterial Proteins; D010544:Peroxidases; C076136:catalase HPI