3D structure and conformational changes in DNA topoisomerase I of Streptococcus pneumoniae

Abstract

Streptococcus pneumoniae is a normal component of the microflora of the human upper respiratory tract and an opportunistic pathogen, however, under appropriate conditions, cause serious and life-threatening infections such as pneumonia, meningitis and septicemia. DNA topoisomerases participate in almost all cellular functions involving DNA transactions, solving the topological problems associated with its replication, transcription, and recombination. Here we report the crystallization and tridimensional structure by X-rays of soluble construct (domain II and III) of S. pneumoniae TopA. The structure showed relevant changes in the domain II in comparison with other topoisomerases solved. This domain can be crucial as target to design new inhibitors for the treatment of S. pneumoniae infections.