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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1662-5. doi: 10.1107/S1744309110042892. Epub 2010 Nov 27.

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 β-trefoil fold and belongs to a well characterized family of carbohydrate-binding modules. Structural analysis of the crystals is in progress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / metabolism
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Lectins / chemistry*
  • Lectins / isolation & purification
  • Lectins / metabolism*
  • Mycobacterium tuberculosis / chemistry*

Substances

  • Bacterial Proteins
  • Lectins