Homology Modeling And Computational Assessment Of Class I Lysyl tRNA Synthetase Of Syphilis Causing Pathogen Treponema Pallidum
D Rao, D VenkataRao, R Ramanjuneyulu
D Rao, D VenkataRao, R Ramanjuneyulu. Homology Modeling And Computational Assessment Of Class I Lysyl tRNA Synthetase Of Syphilis Causing Pathogen Treponema Pallidum. The Internet Journal of Microbiology. 2005 Volume 2 Number 1.
Lysyl-tRNA synthetases (LysRSs) are fashionable amongst the aminoacyl-tRNA synthetases in being composed of unrelated class I and class II enzymes. The prominent role of aminoacyl-tRNA synthetases is to interpret the genetic code in terms of amino acids, providing the essential link between RNA and protein without which translation would be impossible. The recent genomic analysis showed that Class-I Lysyl tRNA synthetase of Archaea is showing similar homology with
The computational approach is assumption that the potential target must play a prominent role in the pathogen's survival and constitute a critical component in its metabolic pathway. At the same time, this target should not have any well-conserved homolog in the host. Drug target identification is essentially subtractive because we use a subtraction template while comparing the two genomes under consideration. The focus is on the complement of the genome of the pathogen that is essential for it but is not present in human. Novel drug targets are required in order to design new defense against antibiotic sensitive pathogens. Multiple approaches to locate essential genes in a given organism exist, some of which focus on the concept that essential genes tend to be evolutionarily conserved over species (Itaya, 1995; Tatusov
Lysyl-tRNA synthetases (LysRSs) are fashionable amongst the aminoacyl-tRNA synthetases in being composed of unrelated class I and class II enzymes. The aminoacyl-tRNA synthetases have long been upheld as an Archaeal type of molecular evolution. This is because their products, aminoacyl-tRNAs, are essentially the same in all living organisms. The prominent role of aminoacyl-tRNA synthetases is to interpret the genetic code in terms of amino acids, providing the essential link between RNA and protein without which translation would be impossible. This highly conserved function has been assumed to place constraints on the evolutionary variation of aminoacyl-tRNA synthetases beyond those enforced on most other protein families.
Most aminoacyl-tRNA synthetases belong to one of two unrelated structural classes. The only widespread exceptions are the lysyl-tRNA synthetases, which are class I enzymes in certain bacteria and archaea but are otherwise members of class II. The class I lysyl-tRNA synthetase is found in a number of pathogenic bacteria (
The solved X-ray structure of Class-I Lysyl tRNA synthetase from
Materials and Methods
The protein sequence of Class-I Lysyl tRNA synthetase of
The results were obtained by the methods mentioned above are summarized. The data of BLAST search results showed that, structure template of
A group of 20 models of Class-I Lysyl tRNA synthetase of
The Best quality model would be expected to have above 90% (Ramachandran 1963). The Bond length and bond angles analysis of overall
In our study, we developed a knowledge based 3D model using computational approach. The structure assessment has been carried out to developed 3D model to evaluate the accuracy of the predicted 3D model folding. The model predicted through this method would helpful to study dynamic nature of Class-I t RNA synthetase in order to find structure and function determinant residues.
There is an urgent need to develop new classes of antibacterial agents to tackle effective drug targets in bacterial pathogens which are unable to grow in
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