Cloning, expression, purification and preliminary X-ray diffraction studies of a putative Mycobacterium smegmatis thiolase.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 67(Pt 7): 817-20, 2011 Jul 01.
Article
in En
| MEDLINE
| ID: mdl-21795802
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 2.5â
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Acetyl-CoA C-Acetyltransferase
/
Mycobacterium smegmatis
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2011
Document type:
Article
Affiliation country:
India