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Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus.

ABSTRACT: Thiaminase type II (TenA) catalyzes the deamination of aminopyrimidines, including the cleavage of thiamine to 4-amino-5-hydroxymethyl-2-methylpyrimidine and 5-(2-hydroxyethyl)-4-methylthiazole in the metabolism of thiamine (vitamin B1), in Staphylococcus aureus (Sa). SaTenA was crystallized by the vapour-diffusion method and the resulting crystal diffracted to 2.6?Å resolution usng synchrotron radiation. The crystal is orthorhombic, belonging to space group P2(1)2(1)2(1) with unit-cell parameters a=103.5, b=104.1, c=109.6?Å. With four molecules in the asymmetric unit, the Matthews coefficient is 2.85?Å3?Da(-1). Initial attempts to solve the structure by molecular-replacement techniques were successful.

SUBMITTER: Begum A

PROVIDER: S-EPMC3079971 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus.

Begum Afshan A Drebes Julia J Perbandt Markus M Wrenger Carsten C Betzel Christian C

Acta crystallographica. Section F, Structural biology and crystallization communications 20101221 Pt 1

Thiaminase type II (TenA) catalyzes the deamination of aminopyrimidines, including the cleavage of thiamine to 4-amino-5-hydroxymethyl-2-methylpyrimidine and 5-(2-hydroxyethyl)-4-methylthiazole in the metabolism of thiamine (vitamin B1), in Staphylococcus aureus (Sa). SaTenA was crystallized by the vapour-diffusion method and the resulting crystal diffracted to 2.6 Å resolution usng synchrotron radiation. The crystal is orthorhombic, belonging to space group P2(1)2(1)2(1) with unit-cell paramete ...[more]

PMID: 21206023

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