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Expression, purification, crystallization and preliminary X-ray analysis of ribitol-5-phosphate cytidylyltransferase from Bacillus subtilis.

ABSTRACT: TarI is a ribitol-5-phosphate cytidylyltransferase that catalyzes the formation of CDP-ribitol, which is involved in the biosynthesis of wall teichoic acids, from CTP and ribitol 5-phosphate. TarI from Bacillus subtilis (BsTarI) was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 1.78?Å and belonged to the monoclinic space group C2, with unit-cell parameters a = 103.74, b = 60.97, c = 91.80?Å, ? = 113.48°. The initial structural model indicated that the crystals of BsTarI contained a dimer in the asymmetric unit.

SUBMITTER: Chen SC

PROVIDER: S-EPMC3497978 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray analysis of ribitol-5-phosphate cytidylyltransferase from Bacillus subtilis.

Chen Sheng-Chia SC Yang Chia Shin CS Lin Ching-Ting CT Chan Nei-Li NL Chang Ming-Chung MC Chen Yeh Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20120926 Pt 10

TarI is a ribitol-5-phosphate cytidylyltransferase that catalyzes the formation of CDP-ribitol, which is involved in the biosynthesis of wall teichoic acids, from CTP and ribitol 5-phosphate. TarI from Bacillus subtilis (BsTarI) was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 1.78 Å and belonged to the monoclinic space group C2, with unit-cell parameters a = 103.74, b = 60.97, c = 91.80 Å, β = 113.48°. The initial structura ...[more]

PMID: 23027746

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