Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei.

Carpena, Xavier; Switala, Jack; Loprasert, Suvit; Mongkolsuk, Skorn; Fita, Ignacio; Loewen, Peter C

Carpena, Xavier; Switala, Jack; Loprasert, Suvit; Mongkolsuk, Skorn; Fita, Ignacio; Loewen, Peter C.

Afiliación

Carpena X; Institut de Biología Molecular de Barcelona CSIC, Jordi-Girona 18-26, 08034 Barcelona, Spain.

Acta Crystallogr D Biol Crystallogr ; 58(Pt 12): 2184-6, 2002 Dec.

Article en En | MEDLINE | ID: mdl-12454496

RESUMEN

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.

Asunto(s)

Proteínas Bacterianas; Burkholderia pseudomallei/enzimología; Peroxidasas/química; Cristalización; Cristalografía por Rayos X; Datos de Secuencia Molecular; Conformación Proteica

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Peroxidasas / Proteínas Bacterianas / Burkholderia pseudomallei Idioma: En Revista: Acta Crystallogr D Biol Crystallogr Año: 2002 Tipo del documento: Article País de afiliación: España Pais de publicación: Estados Unidos

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