• Login
    View Item 
    •   etd@IISc
    • Division of Biological Sciences
    • Molecular Biophysics Unit (MBU)
    • View Item
    •   etd@IISc
    • Division of Biological Sciences
    • Molecular Biophysics Unit (MBU)
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Crystallization and Preliminary Structural Studies on Mycobacterium tuberculosis RuvX

    Thumbnail
    View/Open
    Thesis(Abstract) (6.931Kb)
    Thesis(Full Text) (4.808Mb)
    Author
    Bangalore, Disha Mohan
    Metadata
    Show full item record
    Abstract
    The deadly pathogen Mycobacterium tuberculosis has been characterized for its virulence in immense detail. Regardless of this, the capability of M. tuberculosis to combat extreme stress conditions inside the host cell for extended durations remains unclear. One of the adverse effects caused by host cell mechanisms to the invading M. tuberculosis is DNA damage. Several DNA repair mechanisms exist within the bacterium to counter the DNA damage. The most common type of damage occurring to the genetic material is double stranded breaks (DSBs). Two cardinal pathways exist for the double stranded break repair- Homologous recombination (HR) or Non-homologous end joining (NHEJ) repair pathway. Homologous recombination is more predominant in bacteria and yeast whereas injured mammalian cells are restored by NHEJ. A major intermediate of homologous recombination pathway is Holliday junction. A range of mechanisms act upon HJs for proper chromosome segregation. The process is termed as Holliday junction resolution. A class of enzymes acts on Holliday junction and resolves it into two DNA duplexes. These enzymes are called Holliday junction resolvases. For our study, a Holliday junction resolvase from M. tuberculosis termed as MtRuvX has been chosen. The crystal structure of MtRuvX confirms the presence of RNase H fold in the protein. Docking studies of MtRuvX conducted in this study indicate that the regions interacting with DNA and RNA could be similar. The ATP docking studies also show that there could be two ATP binding sites within the protein. The computational and structural analysis reported here could serve as the foundation for further directed experiments to comprehend the mechanistic details of enzymatic activity of MtRuvX and also its interactions with nucleic acids.
    URI
    https://etd.iisc.ac.in/handle/2005/4044
    Collections
    • Molecular Biophysics Unit (MBU) [301]

    etd@IISc is a joint service of SERC & J R D Tata Memorial (JRDTML) Library || Powered by DSpace software || DuraSpace
    Contact Us | Send Feedback | Thesis Templates
    Theme by 
    Atmire NV
     

     

    Browse

    All of etd@IIScCommunities & CollectionsTitlesAuthorsAdvisorsSubjectsBy Thesis Submission DateThis CollectionTitlesAuthorsAdvisorsSubjectsBy Thesis Submission Date

    My Account

    LoginRegister

    etd@IISc is a joint service of SERC & J R D Tata Memorial (JRDTML) Library || Powered by DSpace software || DuraSpace
    Contact Us | Send Feedback | Thesis Templates
    Theme by 
    Atmire NV