An insight into the active site of a type I DNA topoisomerase from the kinetoplastid protozoan Leishmania donovani.

ABSTRACT: DNA topoisomerases are ubiquitous enzymes that govern the topological interconversions of DNA thereby playing a key role in many aspects of nucleic acid metabolism. Recently determined crystal structures of topoisomerase fragments, representing nearly all the known subclasses, have been solved. The type IB enzymes are structurally distinct from other known topoisomerases but are similar to a class of enzymes referred to as tyrosine recombinases. A putative topoisomerase I open reading frame from the kinetoplastid Leishmania donovani was reported which shared a substantial degree of homology with type IB topoisomerases but having a variable C-terminus. Here we present a molecular model of the above parasite gene product, using the human topoisomerase I crystal structure in complex with a 22

SUBMITTER: Das A 

PROVIDER: S-EPMC100284 | biostudies-literature | 2002 Feb

REPOSITORIES: biostudies-literature