Structure of uracil-DNA glycosylase from Mycobacterium tuberculosis: insights into interactions with ligands.

ABSTRACT: Uracil N-glycosylase (Ung) is the most thoroughly studied of the group of uracil DNA-glycosylase (UDG) enzymes that catalyse the first step in the uracil excision-repair pathway. The overall structure of the enzyme from Mycobacterium tuberculosis is essentially the same as that of the enzyme from other sources. However, differences exist in the N- and C-terminal stretches and some catalytic loops. Comparison with appropriate structures indicate that the two-domain enzyme closes slightly when binding to DNA, while it opens slightly when binding to the proteinaceous inhibitor Ugi. The structural changes in the catalytic loops on complexation reflect the special features of their structure in the mycobacterial protein. A comparative analysis of available sequences of the enzyme from different

SUBMITTER: Kaushal PS 

PROVIDER: S-EPMC2917283 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature