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Cloning, expression, purification, crystallization and preliminary X-ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosis.

ABSTRACT: A secreted lectin, Rv1419, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized and the crystals have been characterized. This represents the first X-ray investigation of a lectin or lectin-like molecule from the pathogen. The cubic crystals contain one molecule in the asymmetric unit. Sequence comparisons indicate that the lectin has a ?-trefoil fold and belongs to a well characterized family of carbohydrate-binding modules. Structural analysis of the crystals is in progress.

SUBMITTER: Patra D

PROVIDER: S-EPMC2998378 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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Cloning, expression, purification, crystallization and preliminary X-ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosis.

Patra Dhabaleswar D Srikalaivani R R Misra Ashish A Singh D D DD Singh D D DD Selvaraj M M Vijayan M M

Acta crystallographica. Section F, Structural biology and crystallization communications 20101127 Pt 12

A secreted lectin, Rv1419, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized and the crystals have been characterized. This represents the first X-ray investigation of a lectin or lectin-like molecule from the pathogen. The cubic crystals contain one molecule in the asymmetric unit. Sequence comparisons indicate that the lectin has a β-trefoil fold and belongs to a well characterized family of carbohydrate-binding modules. Structural analysis of the crystals i ...[more]

PMID: 21139219

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