Cloning, expression, purification and preliminary X - Ray diffraction studies of a putative Mycobacterium smegmatis thiolase

Neelanjana Janardan, Anju Paul, Rajesh K. Harijan, Rikkert K. Wierenga, M. R.N. Murthy

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Thiolases are important in fatty-acid degradation and biosynthetic pathways. Analysis of the genomic sequence of Mycobacterium smegmatis suggests the presence of several putative thiolase genes. One of these genes appears to code for an SCP-x protein. Human SCP-x consists of an N-terminal domain (referred to as SCP2 thiolase) and a C-terminal domain (referred as sterol carrier protein 2). Here, the cloning, expression, purification and crystallization of this putative SCP-x protein from M. smegmatis are reported. The crystals diffracted X-rays to 2.5 Å resolution and belonged to the triclinic space group P1. Calculation of rotation functions using X-ray diffraction data suggests that the protein is likely to possess a hexameric oligomerization with 32 symmetry which has not been observed in the other six known classes of this enzyme.

Original languageEnglish (US)
Pages (from-to)817-820
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number7
DOIs
StatePublished - Jul 2011
Externally publishedYes

Keywords

  • Mycobacterium smegmatis
  • thiolases

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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