Janardan, Neelanjana and Paul, Anju and Harijan, Rajesh K and Wierenga, Rikkert K and Murthy, MRN (2011) Cloning, expression, purification and preliminary X-ray diffraction studies of a putative Mycobacterium smegmatis thiolase. In: Acta Crystallographica Section F, 67 (Part 7). pp. 817-820.Full text not available from this repository. (Request a copy)
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 angstrom 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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to John Wiley and Sons.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||30 Aug 2011 06:36|
|Last Modified:||30 Aug 2011 06:36|
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