Ketkar, Amit D and Shenoy, Avinash R and Kesavulu, Muppuru M and Visweswariah, Sandhya S and Suguna, Kaza (2004) Purification, crystallization and preliminary X-ray diffraction analysis of the catalytic domain of adenylyl cyclase Rv1625c from Mycobacterium tuberculosis. In: Acta Crystallographica Section D: Biological Crystallography, 60 (Part 2). pp. 371-373.
Restricted to Registered users only
Download (184Kb) | Request a copy
The Rv1625c gene product is an adenylyl cyclase identiÆed in the genome of Mycobacterium tuberculosis strain H37Rv. It shows sequence similarity to the mammalian nucleotide cyclases and functions as a homodimer, with two substrate-binding sites at the dimer interface. A mutant form of the catalytic domain of this enzyme, K296E/F363R/D365C (KFD \rightarrow ERC), was overexpressed in Escherichia coli cells in a soluble form. Crystals were obtained using the hanging-drop vapour-diffusion method with PEG 8000 as a precipitant. The protein crystallized in space group $P4_1$, with unit-cell parameters a = b = 71.25, c = 44.51 \AA . X-ray diffraction data were collected to a resolution of 3.4 \AA and the structure has been solved by the molecular-replacement method using a previously built theoretical model of the protein as the search molecule.
|Item Type:||Journal Article|
|Additional Information:||The copyright belongs to International Union of Crystallography.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit
Division of Biological Sciences > Molecular Reproduction, Development & Genetics (formed by the merger of DBGL and CRBME)
|Date Deposited:||30 May 2006|
|Last Modified:||19 Sep 2010 04:27|
Actions (login required)