Investigation of potential hinge region for Mycobacterium tuberculosis topoisomerase I conformational change during catalysis
Abstract
topoisomerase I (MtbTOP1) is essential for the viability of the causative agent of TB. There are still significant unanswered questions regarding the dynamic conformations during catalysis of relaxation of negatively supercoiled DNA by MtbTOP1. We aim to study the flexible hinge residues that control the dynamics of inter-domain rearrangements involved in the enzyme conformational changes that allow the opening-closing of the topoisomerase gate. We used the online server PACKMAN to predict possible hinges from the MtbTOP1 crystal structure. The predicted region "PRO506 to LEU526" at the border between domains D2 and D4 with a p-value
Fields of Study & Subjects
Cancer therapeutics and mechanisms
Enzyme Structure and Function
Protein Structure and Dynamics
Publication details
- Journal / source
- bioRxiv (Cold Spring Harbor Laboratory)
- Publication date
- 5 February 2026
- Language
- EN
- Document type
- Preprint